3201 FPWYKWRLPDVS(3)[30.98 ± 5.84] IPWHRPAQVMHL(3)[27.31 ± 16.09] FPHHKQRYVDPL(3)[6.15 ± 3.98] MHKPTVHIKGPT(2)[21.93 ± 1.84] HTSSLWHLFRST(1)[4.92 ± 0] GMKPWFYSNWKG(1)[1.70 ± 0] GMLHWSYSIFNP(1)[2.01 ± 0] FHRAPWJYLGNY(1)[10.89 ± 8.28] IPLHSLHVKWGK(1)[2.01 ± 0] MGKSTLRYTTIV(1)[31.28 ± 15.03] 10 Phage display (common panning) 3-5 PMID:27861731 Enargite Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Competition experiment Binding assays were performed with selected enargite phage clones in competition with the Wt phage. In these experiments, equal amounts of each phage were mixed and then the usual binding assay was performed. In another experiment, an increasing amount of wild-type phage was added to a constant amount of enargite-binding phage and the assay was performed as with the mini library screen. Screening of a random peptide phage display library resulted in the identification of an enargite-selective peptide with the sequence MHKPTVHIKGPT. Mineral-binding selectivity was demonstrated by binding studies, zeta potential determination and immunochemistry. Peptides that have the ability to discriminate between enargite and chalcopyrite provide a greener option for the separation of arsenic containing contaminants from copper concentrates. This represents the first step towards a major advance in the replacement or reduction of toxic collectors as well as reducing the level of arsenic-bearing minerals in the early stages of mineral processing. 3202 DKKKCDGKRCSWPS(3)[23.91 ± 0] RKKKCKGNCCYTPQ(3)[220.18 ± 55.53] ERSGCHKKACPKTP(2)[68.64 ± 0] HKTQCNPRACTRRH(1)[1.03 ± 0] KKTNCKHDSCRTCQ(1)[12.98 ± 0] QRNKCHHNTCVKML(1)[187.40 ± 87.28] EKDRCTKNTCKPPA(1)[219.02 ± 149.36] KDHDCHRAQCRPNL(1)[41.39 ± 0] GKKKCPNKSCTSLF(1)[10.80 ± 0] KSKSCEAMQCNKYY(1)[5.40 ± 0] KNKRCSQGCCINNG(1)[5.40 ± 0] KNEKCAHHKCYLYP(1)[10.80 ± 0] GKCSCKEKQCRTTL(1)[7.58 ± 0] KSRHCSQIQCGDKV(1)[4.24 ± 0] EKKKCGTMACPYRA(1)[5.19 ± 0] 15 Phage display (common panning) 3-5 PMID:27861731 Chalcopyrite Not determined. Not determined. Not determined. F88-FUSE X4CX4CX4 phage display library (X4CX4CX4) Competition experiment Binding assays were performed with selected chalcopyrite phage clones in competition with the Wt phage. In these experiments, equal amounts of each phage were mixed and then the usual binding assay was performed. In another experiment, an increasing amount of wild-type phage was added to a constant amount of chalcopyrite-binding phage and the assay was performed as with the mini library screen. Screening of a random peptide phage display library resulted in the identification of a chalcopyrite-selective peptide with the sequence RKKKCKGNCCYTPQ. Mineral-binding selectivity was demonstrated by binding studies, zeta potential determination and immunochemistry. Peptides that have the ability to discriminate between enargite and chalcopyrite provide a greener option for the separation of arsenic containing contaminants from copper concentrates. This represents the first step towards a major advance in the replacement or reduction of toxic collectors as well as reducing the level of arsenic-bearing minerals in the early stages of mineral processing. 3203 RCQYPLCS(14/40)[102.96 ± 23.15] RCLRSHCG(3/40)[4.60 ± 0] SCKTVFCY(3/40)[3.77 ± 0] RCPRFSCW(2/40)[10.51 ± 0.40] SCFRPTCP(2/40)[5.01 ± 0] RCQYSPCH(1/40)[4.70 ± 1.99] 6 Phage display (common panning) 3 PMID:27987304 LaPO4:Ce3+,Tb3+, LAP Not determined. Not determined. Not determined. LX-4 phage display library (XCX4CX) Binding assay The percent bound was calculated by dividing the number of eluted phage by the number of input phage and multiplying by 100. Results in Figure 1 are presented as the fold increase above the percent bound of the wild type bacteriophage from up to 6 independent experiments. Data shown were regenerated from Figure 1 in the reference. After three rounds of enrichment, a phage clone containing the surface peptide loop RCQYPLCS was found to bind specifically to LAP. Specificity and affinity of the identified phage bound peptide was confirmed by using binding and competition assays, immunofluorescence assays and zeta potential measurements. Binding and immunofluorescence assays identified the peptide’s affinity for the fluorescent phosphor components CAT (CeMgAl11O19:Tb3+) and BAM (BaMgAl10O17:Eu2+). No affinity was found for other fluorescent phosphor components such as YOX (Y2O3:Eu3+). The binding specificity of the RCQYPLCS peptide loop was improved 3-51-fold by using alanine scanning mutagenesis. The identification of peptides with high specificity and affinity for special components in the fluorescent phosphor in CFLs provides a potentially new strategic approach to rare earth recycling. 3204 GLHTSATNLYLH(7/10)[0.38 ± 0.28] AGYPLSENFYYP(1/10)[4.08 ± 0.31] WQDFGAVRSTRS(1/10)[3.15 ± 0.36] FHPRLQQDHWLH(1/10)[3.92 ± 0.44] 4 Phage display (competitive panning) 3 PMID:28094103 Particulate matter, PM Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Binding assay Spot intensity measurements (with background subtraction) using Image Quant. The data shown were reproduced from the Figure 1B in the reference. Bound phages were eluted using a PM suspension [100 μg PM/ml TBS (50 mM Tris-HCl (pH 7.5), 150 mM NaCl)]. Four PM binding peptides were obtained by phage display and binding characteristics of these peptides were investigated using the peptide array. The strongest binding peptide, WQDFGAVRSTRS, displayed a binding property, measured in terms of spot intensity, 11.4 times higher than that of the negative control, AAAAA. Inductively coupled plasma mass spectrometry (ICPMS) analysis of the transition metal compounds in the PM bound to the peptide spots was performed, and two peptides showed higher binding towards Cu and Zn compounds in PM. These results suggest that the screened peptides could serve as an indicator of transition metal compounds, which are related to adverse health effects, contained in PM. 3205 CHMQGRSTC CHGGQTVAC CNAGHLSQC CTTQMGYSC CPEWFRWHC CNSSASKNC CGWKHEQTC CVPSKPGLC CNSHRHGAC CWWNNFKHC CFPTGTYWC CALHSGQKC CTNASQSYC CNWMINKWC CRDLSLHSC CRTXNGTRC CFSAVVEPC CYKPVRVHC CSLFSKNYC 19 Phage display (common panning) 3 PMID:28414460 SECp43180 Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) 3206 DDGAYTHRSNLI GIWYRDVVQQWP SPGNQTYSSQVR GHGMLILSPNPT GSMAGPENHRAI EPAILTDAMPFN YAPDLLPNSTWT SHVDSASLRYWR SGVYKVAYDWQH GLHTSATNLYLH VHWDFRQWWQPS 11 Phage display (common panning) 3 PMID:28414460 SECp43180 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 3207 TFQAFDLSPFPS(8/17)[2.11 ± 0.07] ISSPRSAPTPPY(6/17)[1.81 ± 0.01] HAPQTFSSPKFP(1/17)[0.34 ± 0.10] WPTYLNPSSLKA(1/17)[0.34 ± 0.07] KLWDIKLPQTSV(1/17)[0.27 ± 0.09] 5 Phage display (common panning) 4 PMID:28349164 Major structural protein VP28 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The binding activities of the positive phage clones to the Envelope protein were measured by phage ELISA. The OD 450nm values were measured and data shown were re-generated from the Figure 1a in the reference. A bacteriophage clone VP28-4L was obtained, and its binding to purified rVP28 protein as well as WSSV from infected shrimp Litopaeneus vannamei tissue was confirmed by ELISA and western blot. The apparent equilibrium dissociation constant (Kd,app) was calculated to be 810 nM. VP28-4L did not show cross-reactivity with any other shrimp viruses. A 12-mer peptide (pep28, with the sequence ′TFQAFDLSPFPS′) displayed on the VP28-4L was synthesized, and its diagnostic potential was evaluated in a lateral flow assay (LFA). Visual detection of WSSV could be achieved using biotinylated-pep28 and streptavidin-conjugated gold nanoparticles. In LFA, 12.5 μg/mL of the virus could be detected from L. vannamei gill tissue homogenate within 20 min. Pep28 thus becomes an attractive candidate in bio-recognition of WSSV in field-usable diagnostic platforms benefitting the aquaculture sector. 3208 KPSHT(12) VNTSN(5) ASSHN(3) 3 Phage display (in vivo) 5 PMID:28359814 Tumor vessels Not determined. Not determined. Not determined. Ph.D.-5 M13 phage display library (X5) Biopanning of the phage-displayed peptide library was performed by in vitro biopanning using human endothelial progenitor cells (hEPCs) and in vivo biopanning in DAS model mice for a total of 3 and 2 rounds, respectively. Phage clones displaying ASSHN peptide showed a marked affinity for hEPCs in vitro, and also for tumor vessels in vivo. PEGylated liposomes modified with the ASSHN peptide (ASSHN-Lip) were designed and prepared for the delivery of anticancer agents. Confocal images showed that ASSHN-Lip clearly bound to hEPCs in vitro and tumor vessels, and also showed extravasation from the vessels. The administration of doxorubicin- encapsulated ASSHN-Lip into Colon26 NL-17-bearing mice significantly suppressed tumor growth compared with doxorubicin-encapsulated PEGylated liposomes. These results suggest that the delivery of anticancer agents with ASSHN-Lip could be useful for targeted cancer therapy. 3209 VTPNDDTFDPFR[38.7 ± 5.4] RPLDLYPGSGQE[85.8 ± 8.3] 2 Phage display (common panning) 3-5 PMID:28475831 Anti-Fumonisins B1 monoclonal antibody Fumonisin B1 Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA Mimotopes, the phage-displayed peptides, A2 (VTPNDDTFDPFR) and D1 (RPLDLYPGSGQE), were tested in competitive ELISAs. Four-parametric logistic fit (OriginPro 9.0) was used to calculate the IC50 values (ng/ml). Clone A2, with peptide sequence VTPNDDTFDPFR, showed the best response in ELISA in terms of sensitivity and reproducibility and was selected for microarray development. A biotinylated synthetic derivative of this mimotope was immobilized onto epoxy-glass slides and fumonisin B1 was detected in a competitive binding inhibition assay using the antifumonisin antibody and a labelled secondary antibody. The array showed an IC50 value of 37.1 ± 2.4 ng mL-1 (n = 9), a detection limit of 11.1 ng mL-1, and a dynamic range from 17.3 to 79.6 ng mL-1. Good specificity towards fumonisin B1 and its structural analog, fumonisin B2, was observed, together with negligible cross-reactivity for other mycotoxins produced by the same fungi species. The mimotope microarray was applied to the analysis of fumonisin B1 in spiked maize and wheat samples. 3210 VHWDFRQWWQPS[1.75 ± 0.12] 1 Phage display (common panning) PMID:28572662 Polystyrene 96-well microtiter plate (polystyrene, PS) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The binding activities of the positive phage clones to polystyrene were measured by phage ELISA. The OD450nm values at the concentration of TBS with 0.20% (w/v) NFM were measured. Data shown were re-generated from the Figure 2 in the reference. Peptide VHWDFRQWWQPS, PB-TUP, has been isolated on target proteins (folate receptor-α, programmed death 1 and programmed death-ligand 1). ELISA and phage recovery assay demonstrated that PB-TUP phage had a significant superior affinity to polystyrene solid surface compared with control phage clones. Propagation rate assays of the selected phage clones showed that the growth rate of PB-TUP phage was not superior to the control phages. Furthermore, the binding of PB-TUB to polystyrene was concentration dependent and varied with solution pH. Molecular modeling revealed that stable structures of α-helix and β-turn may contribute to the binding of PB-TUP to polystyrene plate. The PB-TUP sequence was fused to the N-terminus of peptide P2 and the fusion peptide significantly increased the binding affinity to polystyrene. The fusion peptide also enhanced the cell adhesion ability of peptide P2 with human umbilical vein endothelial cell (HUVEC). The addition of the polystyrene binding peptide provided a convenient method for peptide immobilization. 3211 SGNNPLHVHHDKR 1 Phage display (common panning) 5 PMID:28578326 T lymphocyte leukemia cell line Jurkat Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) By fusing the Jurkat-binding peptide (SGNNPLHVHHDKR) to the C-terminus of IFNα, we constructed an engineered chimeric IFNα molecule (IFNP) for the treatment of adult T-cell leukemia/lymphoma (ATL). We found that IFNP exhibited significantly higher activity than wild type IFNα in inhibiting the growth of leukemia cells and inducing cell blockage at the G0/G1 phase. The synthetic IFNP molecule exerted its antitumor activity by upregulating the downstream genes involved in the STAT1 pathway and in apoptosis. Using a cell receptor binding assay, we showed that this Jurkat-binding peptide facilitated the binding affinity of IFNα to the cell surface type I IFN receptor. The engineered IFNP molecule may prove to a novel antitumor approach in the treatment of patients with ATL. 3212 CNYCRLNLW(19)[0.36 ± 0.07] CRSTLQHSC(1)[0.27 ± 0.05] CLKNQSDQC(1)[0.20 ± 0.04] CSTSSRTGC(1)[0.04 ± 0.01] CMHVRHGLV(1)[0.16 ± 0.04] CDSAPTRKC(1)[0.16 ± 0.04] 6 Phage display (subtractive panning) 3 PMID:28584144 Nitrite reductase AniA Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) ELISA Phage clones were purified and tested separately to measure their affinity to sAniA in the phage ELISA assay. Absorbance at 450 nm was measured. Readings were compared to wells, which underwent identical treatment but lacked sAniA (control) and to signal from a wild type phage, M13KE (of 1010 PFU), that does not display peptides (wild type). The mean and SEMs from seven independent experiments are shown. Data shown were re-generated from Figure 3C in the reference. Magnetic Ni-NTA bead based affinity capture was used to immobilize sAniA. A preclearance step was to remove Ni2+ and plastic binders from the phage pool. 3213 AYPPNLWQKALA(2)[0.21 ± 0.04] HLNHNDNYLPP(1)[0.14 ± 0.04] AYSDRIPSLWDT(1)[0.07 ± 0.04] GYIERGLALWNS(1)[0.50 ± 0.10] YNFDVWKDHWIY(1)[0.24 ± 0.08] KHYYGGDTTTLW(1)[0.22 ± 0.06] SYNFDLWSFGLE(1)[0.68 ± 0.03] HYDRGNLWFQKS(1)[0.17 ± 0.06] GYKVPLWSKPEY(1)[0.11 ± 0.03] AQYERFDWASWW(1)[0.16 ± 0.04] YPSTLREMFWH(1)[0.35 ± 0.07] THDFSKARLWPS(1)[0.36 ± 0.06] EYSSFRLWNIYT(1)[0.53 ± 0.08] YHDLNLWELNVR(1)[0.34 ± 0.06] YHPNGMNPYTKA(1)[0.50 ± 0.08] DYSKMRLWDLRP(1)[0.14 ± 0.04] SYKYPLWHSITL(1)[0.22 ± 0.04] SLSPHYMNLWNA(1)[0.29 ± 0.06] YTGRAIDLWTEW(1)[0.24 ± 0.06] QYPYDLWSSMQR(1)[0.43 ± 0.09] SMSYKDREMQMW(1)[0.21 ± 0.04] AYSEWYASLWDF(1)[0.53 ± 0.09] ASIYYKDRSLLW(1)[0.53 ± 0.11] 23 Phage display (subtractive panning) 3 PMID:28584144 Nitrite reductase AniA Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA Phage clones were purified and tested separately to measure their affinity to sAniA in the phage ELISA assay. Absorbance at 450 nm was measured. Readings were compared to wells, which underwent identical treatment but lacked sAniA (control) and to signal from a wild type phage, M13KE (of 1010 PFU), that does not display peptides (wild type). The mean and SEMs from seven independent experiments are shown. Data shown were re-generated from Figure 3C in the reference. Magnetic Ni-NTA bead based affinity capture was used to immobilize sAniA. A preclearance step was to remove Ni2+ and plastic binders from the phage pool. 3214 HSVKPVVNLILR(34) HSIRLHTYPHMK(19) YSLRADSRWMPS(18) HSLRPEWRMPGP(15) HSIRTYWQSAQP(10) HSLKPSWLLLGY(2) HSLKPSLKQLAI(2) HSLREDWTLRMQ(2) APPGNWRNYLMP(2) TMGFTAPRFPHY(2) TMHSLRPEWRMP(1) HSVKPDWAQMLR(1) HSVKHDFRLLTK(1) HSIRSSHLHMFT(1) SGHQLLLNKMPN(1) APRLPQSLLPQL(1) SHALPLTWSTAA(1) APPMSRQSFDGV(1) NFMESLPRLGMH(1) LLADTTHHRPWT(1) MEGQYKSNLLFT(1) NTELTSYGPPPA(1) H-S-[ILV]-[KR],[KR]-X-P, [KR]-X-X-P 22 Phage display (subtractive panning, competitive panning) 4 PMID:28415614 Gap junction alpha-5 protein Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) A phage library was first pre-cleared in an uncoated well, and then presented to the bait protein. Low-affinity binders were first eluted using a solution of free bait protein in TBS. One of the retrieved peptides (HSLRPEWRMPGP) showed a 58.3% homology with amino acids 5-to-16 of IκBα, a member of the protein complex inhibiting NFκB activation. Binding of IκBα (peptide) and Cx40 was confirmed by crosslinking and en face proximity ligation assay on carotid arteries. 3215 GASESYL 1 Phage display (common panning) PMID:28208072 Anti-triosephosphate isomerase (TIM) polyclonal antibody Triosephosphate isomerase, TIM Not determined. Not determined. Ph.D.-7 phage display library (X7) A conformational epitope (A71G74S69D75T73F72V67) was confirmed by the phage display technology. 3216 CKKKAGSGC(57) CKELRDMQC(54) CDAPRSRRC(47) CKGKGRKGC(41) CGKKESPRC(40) CNKSMRNSC(39) CNKQARAKC(38) CERAQNGGC(37) CTGRDGKSC(36) CVNQVGKRC(35) CRKVKGDKC(30) CKKGLKGKC(20) CREGKGVRC(20) CKKKESSRC(18) CKGGKGARC(16) CRDTGEEKC(16) CKSEHVKKC(16) CKGKNSGRC(15) CKKSGGKKC(15) CKGAEEKKC(15) CREKRDNKC(14) CRSNMREKC(13) CKRDLSRRC(13) CKGSVNKRC(13) [RK]-x(2)-[RK], C-[RK]-x(5)-[RK]-C 24 Phage display (in vivo) 3 PMID:28468593 Human gastric cancer cell line MKN-45P Not determined. Not determined. Not determined. CX7C T7 phage display library For ex vivo biopanning, 1.0e10 pfu of CX7C phage naïve library was incubated with tumor and organs excised from the mice with MKN-45 IP tumors. For in vivo biopanning, amplified phage pool from previous round was IP injected to an MKN-45 tumor mouse and incubated for 1 h. After the termination, tumors and organs were collected, washed with DMEM, and transferred in LB-NP40. The rescued phage was amplified, pooled, and used for the subsequent round of selection. IP3 peptide with the sequence of CKRDLSRRC was identified by in vivo phage display on a mouse model of peritoneal carcinomatosis of gastric origin (MKN-45P), using high-throughput sequencing of the peptide-encoding region of phage genome as a readout. The IP3 peptide contains a hyaluronan-binding motif, and fluorescein-labeled IP3 peptide bound to immobilized hyaluronan in vitro. After intraperitoneal administration in mice bearing peritoneal metastases of gastric and colon origin, IP3 peptide homed robustly to macrophage-rich regions in peritoneal tumors, including poorly vascularized micro-tumors. Finally, we show that IP3 functionalization conferred silver nanoparticles the ability to home to peritoneal tumors of gastric and colonic origin, suggesting that it could facilitate targeted delivery of nanoscale payloads to peritoneal tumors. Collectively, our study suggests that the IP3 peptide has potential applications for targeting drugs, nanoparticles, and imaging agents to peritoneal tumors. 3217 CKKGLKGKC(225) CVNQVGKRC(209) CRDTGEEKC(159) CTGRDGKSC(123) CERAQNGGC(84) CKELRDMQC(45) CKGKGRKGC(38) CKGKNSGRC(32) CREGKGVRC(28) CKSEHVKKC(20) CKGGKGARC(18) CKGAEEKKC(16) CKKKAGSGC(15) CNKQARAKC(15) CRSNMREKC(3) CGKKESPRC(2) CNKSMRNSC(2) CRKVKGDKC(2) 18 Phage display (in vivo) 3 PMID:28468593 Mouse colon adenocarcinoma cell line CT26 Not determined. Not determined. Not determined. CX7C T7 phage display library 3218 CKKKAGSGC(83) CKELRDMQC(80) CKKSGGKKC(77) CNKQARAKC(69) CKGGKGARC(62) CKGKGRKGC(56) CTGRDGKSC(55) CVNQVGKRC(50) CRKVKGDKC(36) CERAQNGGC(24) CNKSMRNSC(23) CRDTGEEKC(21) CREGKGVRC(20) CGKKESPRC(18) CKKGLKGKC(18) CKSEHVKKC(14) CKGKNSGRC(9) CKGSVNKRC(5) CREKRDNKC(4) CRSNMREKC(3) CDAPRSRRC(2) CKKKESSRC(2) CKGAEEKKC(2) CKRDLSRRC(2) 24 Phage display (in vivo) 3 PMID:28468593 Kidney Not determined. Not determined. Not determined. CX7C T7 phage display library 3219 CQNNNMTSC(47.4%) CNWGDRILC(31.6%) CTVRTSADC(15.8%) CIGNSNTLC(5.30%) 4 Phage display (subtractive panning) 5 PMID:28428053 Crohn disease (CD) inflamed mucosa Not determined. Not determined. Not determined. Ph.D.-7 and Ph.D.-C7C phage display library pool A subtraction step was performed initially by clearing non-specific binders against a freshly harvested normal colon mucosa of healthy volunteers undergoing colonoscopy. We identified one peptide (TVRTSAD) able to recognize selectively biopsies of inflamed mucosa of Crohn disease (CD) patients. 3220 CNWGDRILC(31.3%) CQNNNMTSC(31.3%) CIGNSNTLC(12.5%) CWPANTLKC(12.5%) 4 Phage display (subtractive panning) 5 PMID:28428053 Ulcerative colitis (UC) inflamed mucosa Not determined. Not determined. Not determined. Ph.D.-7 and Ph.D.-C7C phage display library pool A subtraction step was performed initially by clearing non-specific binders against a freshly harvested normal colon mucosa of healthy volunteers undergoing colonoscopy. We identified one peptide (WPANTLK) able to recognize selectively biopsies of inflamed mucosa of ulcerative colitis (UC) patients. 3221 CTNPGVHIC(54.5%) CLKLGEKWC(18.2%) 2 Phage display (common panning) 5 PMID:28428053 Normal colon mucosa of healthy volunteers Not determined. Not determined. Not determined. Ph.D.-7 and Ph.D.-C7C phage display library pool 3222 GAMHLPWHMGTL(3/13) GAMHLSWHMGTH(1/13) DPMHNNWHSSPI(1/13) GLDHLWWSSQTP(1/13) NPWEEQGYRYSM(1/13) NPWNEMWFQTSR(1/13) NNPWREMMYIEI(1/13) WADMMTSVTPWL(1/13) SEFPRSWDMETN(1/13) QHYETLAFRPKH(1/13) ATYNSVNRHSAV(1/13) 11 Phage display (common panning) 4/5 PMID:28529640 Huamn large cell carcinoma (LCC) cell line H460 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Three targeting phages (HPC1, HPC2, and HPC4) and their respective displayed peptides (GAMHLPWHMGTL, NPWEEQGYRYSM and NNPWREMMYIEI) were able to bind to both SCLC and NSCLC cell lines, as well as clinical specimens, but not to normal pneumonic tissues. In vivo optical imaging of phage homing and magnetic resonance imaging (MRI) of peptide-SPIONs revealed that HSP1 was the most favorable probe for multimodal molecular imaging. Using HSP1-SPION, the T2-weighted MR signal of H460 xenografts was decreased up to 42%. In contrast to the tight binding of HSP1 to cancer cell surfaces, NNPWREMMYIEI was preferentially endocytosed and intracellular drug delivery was thereby effected, significantly improving the therapeutic index of liposomal drug in vivo. Liposomal doxorubicin (LD) conjugated to GAMHLPWHMGTL, NPWEEQGYRYSM or NNPWREMMYIEI had significantly greater therapeutic efficacy than non-targeting liposomal drugs in NSCLC (H460 and H1993) animal models. Combined therapy with an NNPWREMMYIEI-conjugated stable formulation of liposomal vinorelbine (sLV) further improved median overall survival (131 vs. 84 days; P = 0.0248), even in aggressive A549 orthotopic models. Overall, these peptides have the potential to guide a wide variety of tailored theranostic agents for targeting therapeutics, non-invasive imaging, or clinical detection of SCLC and NSCLC. 3223 DYDRYSSALIAA(5)[0.42] GQPKTFLSVSEL(5)[0.14] YWTPGYTPSQTE(1)[NA] NNSRDTALRWFV(1)[NA] 4 Phage display (common panning) 3 PMID:28469983 Anti-HO-1 polyclonal antibody Heme oxygenase-1, HO-1 Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The selection of positive phage clones specific to polyclonal anti-△rHO-1 antibodies was detected by competitive ELISA. The color intensity was determined spectrophotometrically at A450. Data shown were reproduced from Figure 3 in the reference. NA denotes not applicable. Screening of a phage display library revealed four epitopes that could interact with the polyclonal antibody prepared by immunizing rabbits with the purified HO-1 protein. Two of these four epitopes (DYDRYSSALIAA and GQPKTFLSVSEL) are responsible for HO-1 catalytic activity because their antibodies were able to neutralize HO-1 activity. 3224 KCCFPAQ(13) SILPYPY(4) YPAPWPP(3) QPWPTSI(3) WPTPPYA(1) MHAPPFY(1) 6 Phage display (subtractive panning) 5 PMID:28012848 Human colorectal cancer cell line HT29 Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) Three rounds of biopanning with a total of ~1e9 plaque-forming units (pfu) was performed with ~1e6 human normal intestinal cells Hs738.St/Int (control) to remove non-specific binders. The supernatant containing the cleared phage pool was amplified to ~2e11 pfu for positive selection against HT29 cells. We identified the peptide sequence KCCFPAQ, and measured an apparent dissociation constant of kd = 72 nM and an apparent association time constant of k = 0.174 min–1 (5.76 min). During fluorescence imaging of patients during endoscopy, regions of SSA had 2.43-fold higher mean fluorescence intensity than that for normal colonic mucosa. Fluorescence labeling distinguished SSAs from normal colonic mucosa with 89% sensitivity and 92% specificity. The peptide had no observed toxic effects in animals or patients. In the analysis of ex vivo specimens, peptide bound to SSAs had significantly higher mean fluorescence intensity than to hyperplastic polyps. 3225 NPVEDYLDYSVI ESYYMNPVEMFV LPTESNPVEDWI NPIESYIASVFS NPVELLLKTSSD NPVETQIVLSLV NPVEKWISMRTM NPVELLLLMGIS NGIERLLEEPVS NPVENWIDPKSI VNPVEYYLDTMR NPVEALLSKFHM NPVESYLANYTS VTNPYESLVQEK SPPEFSGSTVGL MVPEFSGSFPMR RMPPEFMGSLPQ QLFVPEFAGSSP LVPEFTGSTPFR SHGAIEFDGAFP VPEFAGHVPSTA VPEMNGSLIARK HPIVKTYFAQTT APAKTYFGQTTD QMKAWFPQTTYD ATKVMFPQRIYV QPAKTYFNQVTL QAAAKTMFPQNT SPSIDAFETSIF SWVLTATETGSS EMRFPSLSASDT QAPTLDAQETAL TALDAVSTGFSW GAIGSLTADSTS SLGSLSAYETGR TLYRPPLTSAET LIADLNAESTSR SLGAAGARVTTV ASGPLHAGATGL GHKPVLTALSTA VMPAIHAGVTGA VHPTLTVTSKEI ELDVSLRVMPKV SKLAMEIMSGPV SNAVTSSKSPRM QADATVLTKPKT KAVSDASRGTVF DYPKIANFQEYA GGQVRSIHSGPT QHWPTNVDSVTV ETKSDDMLLSNV MTVDRTVRVASK DLLIRDAITDTK AYHVDTVSDAGW VDTINLPQNTIQ VMSVNASTTAAN TLHAPMTIRSGP TNLHRVMTVVNM LRPNAVQTDTLA QMRQLTEYGSEK VLSSTAIKVDSV VHTVHDVFTAFG AKIRMFLDTDYK ASWGPIAIDRVN SQQYALTNSTTN QPQTKSFYPQYV NVVDRVNRTGVV WSALPERTSLPV RPAIVDQVSSSP QWNWRVRSVANV AQLHPTTLVKHK TSYRPPLNVCQD QSHSLFYPHPYG N-P-V-E-x(3), X-P-E-F-X-G-S-x(2), K-x(2)-F-P-Q-x-T 73 Phage display (common panning) 3 PMID:28167275 Human whole serum Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) We synthesize identified peptides in the array format and rescreen the serum used for phage panning to validate antibody binding peptides. Finally, we systematically vary the sequence of validated antibody binding peptides to identify those amino acids within the peptides that are crucial for binding “their” antibody species. The resulting immune fingerprints can then be used to trace them back to potential antigens.