1701 RHTDGLRRIAAR(1) RTRRQGGDVSRD(1) RPRRSAARGSEG(1) ADRTRGRIRGNC(1) NTVWRLNSSCGM(1) EKWGMHQECYRH(1) TMEPRWWCNPIN(1) R-x-R-R 7 Bacterial display (common panning) 5 PMID:15236241 Cuprous oxide, Cu(2)O Not determined. Not determined. Not determined. FliTrx bacterial display library (X12) To recover binders, the surface was moved to a sterile culture dish containing 10 mL of IMC supplemented with carbenicillin and the plate was vortexed for 30 s to shear off the flagella. Peptides binding electrodeposited Cu(2)O with high avidity could be subdivided into two classes based on pI and hydrophilicity. In the hydrophilic and positively charged Class I binders, the Arg-X-X-Arg tetrapeptide appears to be implicated in metal oxide binding. Molecular dynamics simulations of the disulfide-constrained peptides suggest that the aforementioned motifs are important to properly orient two basic residues that are likely to contact the metal oxides. 1702 RIGHGRQIRKPL(1) VRTRDDARTHRK(1) PASRVEKNGVRR(1) MRHSSSGEPRLL(1) PAGLQVGFAVEV(1) RTDDGVAGRTWL(1) R-x(2)-R-K 6 Bacterial display (common panning) 5 PMID:15236241 Zinc oxide, ZnO Not determined. Not determined. Not determined. FliTrx bacterial display library (X12) To recover binders, the surface was moved to a sterile culture dish containing 10 mL of IMC supplemented with carbenicillin and the plate was vortexed for 30 s to shear off the flagella. Peptides binding electrodeposited ZnO with high avidity could be subdivided into two classes based on pI and hydrophilicity. In the hydrophilic and positively charged Class I binders, the Arg-X-X-Arg tetrapeptide appears to be implicated in metal oxide binding. Molecular dynamics simulations of the disulfide-constrained peptides suggest that the aforementioned motifs are important to properly orient two basic residues that are likely to contact the metal oxides. 1703 GMFTRNWCSRTFWCR(1) FIADPERYWCSVPAL(1) WYPVSWTKNLWYGPK(1) MCYYSRCNIMTCLSN(1) KYTWYGYSLRANWMR(1) RILCYAHARNRFIFN(1) 6 Bacterial display (common panning) PMID:17469847 Human red blood cells, RBCs Not determined. Not determined. Not determined. X15 E. coli bacterial display library To enrich for binding clones prior to screening by FACS, bacteria were incubated with human RBCs and washed to remove unbound bacteria. RBC-bound bacteria were then amplified by growth. Plasmid DNA was isolated from the first round pool and transformed into an E. coli MC1061 strain expressing green fluorescent protein (GFP), enabling subsequent rounds of screening using FACS. Since the bacteria used in the final two rounds of selection were fluorescent, RBCs were fluorescently labeled if bacteria were bound to the RBC membrane. RBCs binding to fluorescent bacteria were sorted by FACS, and the recovered bacteria were amplified by growth. Among isolated clones exhibiting binding to RBCs, six clones exhibiting the highest RBC labeling, as measured by flow cytometry, were selected for further analysis. Each of the isolated bacterial clones yielded greater than a 75-fold increase in RBC labeling relative to nonbinding cells displaying only the OmpA scaffold (i.e., without a peptide insertion). Clones GMFTRNWCSRTFWCR and KYTWYGYSLRANWMR bound most extensively to RBCs, resulting in more than 200-fold increased binding. 1704 GLVLETVGSGAR(1) CEAAQMVRPWVY(1) RSVSLSKSVAGV(1) GMEFGRRKRDVN(1) GARRHEIRGVDV(1) TDRSPRGVMRHA(1) 6 Bacterial display (common panning) PMID:18977188 Titanium dioxide, TiO2 Not determined. Not determined. Not determined. FliTrx bacterial display library (X12) Selection of proteins was carried out on a silicium wafer sputtered with TiO2 in anatase conformation. To verify binders and to analyze the binding kinetics of the diluted suspension of the purified proteins, the chip-based S-sens K5 surface acoustic wave sensor system was used. To recover binders, the surface was moved to a sterile culture dish containing 10 mL of IMC supplemented with carbenicillin and the plate was vortexed for 1 min to shear off the flagella. For peptide CGPGLVLETVGSGARGPC, the binding kinetics was analyzed. On- and off-rate binding constants were extracted from the fitted curves. With the resulting association rate constant k(on) and the dissociation constant k(off), the affinity of the peptide for the TiO2 surface was calculated, represented by the equilibrium dissociation constant K(D) = 81 nM. 1705 VRRSKHGARKDR[191] 1 Bacterial display (common panning) PMID:19048606 Heparin Not determined. Not determined. Not determined. FliTrx bacterial display library (X12) Surface plasmon resonance (SPR) The evaluation of the kinetic parameters was performed using a SPR-based BIAcoreX biosensor (BIAcore). The dissociation constant (KD =kd/ka, nm) is shown. Isolated insert analysis revealed a novel heparin-binding peptide sequence, VRRSKHGARKDR, designated as HBP12. Our analysis of the sequence alignment of heparin-binding motifs known as the Cardin-Weintraub consensus (BBXB, where B is a basic residue) indicates that the HBP12 peptide sequence contains two consecutive heparin-binding motifs (i.e. RRSK and RKDR). SPR-based BIAcore technology demonstrated that the HBP12 peptide binds to heparin with high affinity (K(D) = 191 nM). The HBP12 peptide is found to bind the cell surface HS expressed by osteoblastic MC3T3 cells and promote HS-dependent cell adhesion. Moreover, the surface-immobilized HBP12 peptide on titanium substrates shows significant increases in the osteoblastic MC3T3-E1 cell adhesion and proliferation. 1706 CHKRSFWADNC(1)[11.0, 10.9, 9.42] CRTQFRPNQTC(1)[10.1, 13.3, 13.9] CQLCDFWRTRC(1)[6.05, 8.72, 6.63] CFEDFNEQRTC(1)[1.68, 4.02, 3.50] CQNWIKDVHKC(1)[15.8, 19.4, 13.1] CLAKFLKGKDC(1)[NT] CWHRRTHKTFC(1)[NT] CRTIQTRSHWC(1)[NT] CIKLAQLHSVC(1)[NT] CWRHRNATEWC(1)[NT] 10 Bacterial display (common panning) PMID:20025916 IgG from human, mouse, rat, rabbit and goat Not determined. Not determined. Not determined. CX9C E. coli bacterial display library Surface plasmon resonance (SPR) The binding affinities of the selected peptides for human IgG, mouse IgG and rabbit IgG were determined using SPR analysis, respectively. SPR measurements were performed on a CM5 sensor chip. The binding constants (μM) were shown. FcBP1, DCAWHLGELVWCT, was used as positive control and its kinetic constants for human IgG, mouse IgG and rabbit IgG were 0.848, 0.732 and 1.69 μM, respectively. NT denotes not tested. The binding affinities of the selected peptides for IgGs were determined using SPR analysis. Five novel peptides were identified as potential affinity ligands for IgG purification. 1707 KMRAWGHPIWNW TKHGKRSRCYNL 2 Yeast display (common panning) 7 PMID:17238208 C crystalline face of synthetic sapphire, α-Al(2)O(3) Not determined. Not determined. Not determined. PL12 yeast display library (X12) Biopanned cells, each expressing a unique peptide, were agitated in the presence of sapphire surface, and then loosely bound cells were removed by surface washing. The adherent cells were then grown off the surface to create a subpopulation used in the subsequent round of biopanning. Twenty-four clones from sub-populations in the last round were sequenced. 1708 RTAKRKWKHTRD 1 Yeast display (common panning) 7 PMID:17238208 A crystalline face of synthetic sapphire, α-Al(2)O(3) Not determined. Not determined. Not determined. PL12 yeast display library (X12) Biopanned cells, each expressing a unique peptide, were agitated in the presence of sapphire surface, and then loosely bound cells were removed by surface washing. The adherent cells were then grown off the surface to create a subpopulation used in the subsequent round of biopanning. Twenty-four clones from sub-populations in the last round were sequenced. 1709 RTAKRKWKHTRD KRHKQKTSRMGK KRSKKCLRKNGS 3 Yeast display (common panning) 7 PMID:17238208 R crystalline face of synthetic sapphire, α-Al(2)O(3) Not determined. Not determined. Not determined. PL12 yeast display library (X12) Biopanned cells, each expressing a unique peptide, were agitated in the presence of sapphire surface, and then loosely bound cells were removed by surface washing. The adherent cells were then grown off the surface to create a subpopulation used in the subsequent round of biopanning. Twenty-four clones from sub-populations in the last round were sequenced. 1710 MEMNKVWRDLAA(1) IDQDKFWRELGS(1) LEGDKVWLEVRS(1) IEVDKVQHDLLS(1) FDEHKLWYELAA(1) LDVDKFREEVAS(1) 6 Yeast display (common panning) 2 PMID:19863063 Lipoate-protein ligase A Not determined. Not determined. Not determined. LAP yeast display library 1711 LERNKVWYEIKA(1) IEVDKSWLELRS(1) MELDKAWVEVWS(1) IDIDKIWYEFGS(1) FENDKIWHDIWA(1) IQGDKIWTELDS(1) FEYDKVWVDLPA(1) 7 Yeast display (common panning) 3 PMID:19863063 Lipoate-protein ligase A Not determined. Not determined. Not determined. LAP yeast display library 1712 FELDKVWFDVDS(1) FEIDKVWHDFPA(2) FEHEKVWYDLCA(5) FEINKVWFELLA(3) 4 Yeast display (common panning) 4 PMID:19863063 Lipoate-protein ligase A Not determined. Not determined. Not determined. LAP yeast display library The clones were obtained from high phycoerthyrin gate (Gate A). 1713 VEHDKVFYEFDS(1) IEIDKVWHDLYS(1) LEIDKVWHELDS(1) IELYKVWYEIDA(1) LEEDKIWYEFEA(1) VERDKVWYDISS(1) MERAKVWYELEA(1) 7 Yeast display (common panning) 4 PMID:19863063 Lipoate-protein ligase A Not determined. Not determined. Not determined. LAP yeast display library The clones were obtained from low phycoerthyrin gate (Gate B). 1714 YPSAPPQWLTNT(16) STPLVTGTNNLM(8) QSGSHVTGDLRL(2) ATTLHPPRTSLP(1) WPYAASNALVSP(3) AEMAAPTGLQVK(1) HLPTSSLFDTTH(1) 7 Phage display (subtractive panning) 5 DOI:10.1039/B806797J Titanium dioxide, TiO2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Peptide-bearing phage particles that bind to silica were first removed from the library by incubation with the diatom silica. The fourth and fifth rounds of such biopanning were conducted using 0.8% TBST washing solutions, in order to increase the stringency of selection for titania-binding phage. While prior phage display biopanning with silica and titania targets has led to the isolation of polycationic peptides enriched in basic residues, the subtractive biopanning process yielded several acidic peptides enriched in hydroxyl-bearing residues. These peptides were found to induce the precipitation of titania, but not silica, from aqueous precursor solutions at pH 3-8. 1715 CNKHQPMHC(1) CQNPMQTFC(1) CNQLSTRPC(1) CNNKVPVLC(1) CLQNRQSQC(1) CQLQRQWNC(1) CQVNSAHQC(1) 7 Phage display (common panning) 3 DOI:10.1039/B307593A Zinc sufide, ZnS Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Isolated ZnS binding motifs contained arrangements of positively charged groups (R, H, K), proline (a structural amino acid), and methionine residues. 1716 CQSMPHNRC(1) CFPMRSNQC(1) CPPQPNRQC(1) CNHQMPMQC(1) CNRQAVNAC(1) 5 Phage display (common panning) 4 DOI:10.1039/B307593A Zinc sufide, ZnS Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Isolated ZnS binding motifs contained arrangements of positively charged groups (R, H, K), proline (a structural amino acid), and methionine residues. 1717 CHMAPRWQC(1) CQSMPHNRC(2) CNNPMHQNC(3) 3 Phage display (common panning) 5 DOI:10.1039/B307593A Zinc sufide, ZnS Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Isolated ZnS binding motifs contained arrangements of positively charged groups (R, H, K), proline (a structural amino acid), and methionine residues. 1718 RRQDVHLPSRTL LRRSSEAHNSIV LPRAFMGHAPGS TRHMASRTEAHL LPPAWAMQVHTA PRPSPKMGVSVS 6 Phage display (common panning) DOI:10.1039/B307593A Zinc sufide, ZnS Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The peptide sequence typically had a combination of a positively charged amino acid group and a proline, followed by either a methionine, or a hydroxyl containing amino acid group. 1719 QNPIHTH 1 Phage display (common panning) DOI:10.1039/B307593A Lead sulphide, PbS Not determined. Not determined. Not determined. Ph.D.-7 phage display library (X7) 1720 CTYSRLHLC 1 Phage display (common panning) DOI:10.1039/B307593A Cadmium sulfide, CdS Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) 1721 PWIPTPRPTFTG SLTPLTTSHLRS 2 Phage display (common panning) DOI:10.1039/B307593A Cadmium sulfide, CdS Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) 1722 SCFWFLRWSLFIVLFTCCS(1) SCESVDCFADSRMAKVSMS(1) SCVGFFCITGSDVASVNSS(1) SCSDCLKSVDFIPSSLASS(1) SCAFDCPSSVARSPGEWSS(1) SCMLFSSVFDCGMLISDLS(1) SCVDYVMHADSPGPDGLNS(1) SCSENFMFNMYGTGVCTES(1) SCSSFEVSEMFTCAVSSYS(1) SCGLNFPLCSFVDFAQDAS(1) 10 Phage display (common panning) 3 DOI:10.1002/adma.200700029 6Al-4V Ti Not determined. Not determined. Not determined. SC-X(16)-C M13 phage display library 1723 KSLSRHDHIHHH TQHLSHPRYATK SRPSRQPSASPT LLADTTHHRPWT 4 Phage display (common panning) 5 DOI:10.1021/cm071515t (001)-oriented TiO2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. 1724 MRMIRRFPSSLK TQHLSHPRYATK LKMNPSISSSLK FAVNPSKPAYFK FTTSNHTSRHGS YPMLPQNKHAQF QNLINWPPPRFS NVTTMTNHLVYS LATPFTATSATG 9 Phage display (common panning) 5 DOI:10.1021/cm071515t (100)-oriented TiO2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round. 1725 RKKRTKNPTHKL KSLSRHDHIHHH TQHLSHPRYATK ASIEELRVPRQA NHHHQPLARNQS LLPQNGSTPRHS SFSAITKNVHWM TFSNPLYMWPRP SPGLSLVSHMQT SAHGTSTGVPWP 10 Phage display (common panning) 5 DOI:10.1021/cm071515t (110)-oriented TiO2 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) A 0.2% TBST wash solution was used to remove phages with low binding affinity to titania during the first four rounds, whereas a more stringent 0.5% TBST wash solution was used for the fifth round.