biostudies-literatureMajumdar SNIGMS NIH HHS5937-40https://www.ebi.ac.uk/biostudies/studies/S-EPMC2597205biostudies-literatureUnknown18(22)Phage display of protein and peptide libraries offers a powerful technology for the selection and isolation of ligands and receptors. To date, the technique has been considered limited to soluble, non-membrane proteins. We report two examples of phage display of full-length, folded and functional membrane proteins. Consistent display required the recently reported KO7(+) helper phage. The two proteins, full-length caveolin-1 and HIV gp41, display well on the surface of the phage, and maintain their binding activities as shown by in vitro assays.Bioorganic & medicinal chemistry lettersPhage display of functional, full-length human and viral membrane proteins.PMC2597205GM-069337T34 GM069337R01 GM078528Majumdar SMendez ASHajduczki AWeiss GAfalsePhage display of functional, full-length human and viral membrane proteins.Phage display of protein and peptide libraries offers a powerful technology for the selection and isolation of ligands and receptors. To date, the technique has been considered limited to soluble, non-membrane proteins. We report two examples of phage display of full-length, folded and functional membrane proteins. Consistent display required the recently reported KO7(+) helper phage. The two proteins, full-length caveolin-1 and HIV gp41, display well on the surface of the phage, and maintain their binding activities as shown by in vitro assays.2008-01-01T00:00:00Z2008 Nov2026-03-16T16:28:55.163Z2025-08-31T03:05:28.184ZS-EPMC25972051866730610.1016/j.bmcl.2008.07.051