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Background/purpose: The VPAC1 receptor, a member of the vasoactive intestinal peptide receptors (VIPRs), is overexpressed in the most frequently occurring malignant tumors and plays a major role in the progression and angiogenesis of a number of malignancies. Recently, phage display has become widely used for many applications, including ligand generation for targeted imaging, drug delivery and therapy. In this work, we developed a panning procedure using a phage display peptide library to select a peptide that specifically binds to the VPAC1 receptor to develop a novel targeted probe for molecular imaging and therapy.

Methods: CHO-K1 cells stably expressing VPAC1 receptors (CHO-K1/VPAC1 cells) were used to select a VPAC1-binding peptide from a 12-mer phage peptide library. DNA sequencing and homologous analysis of the randomly selected phage clones were performed. A cellular ELISA was used to determine the most selectively binding peptide for further investigation. Binding specificity to the VPAC1 receptor was analyzed by competitive inhibition ELISA and flow cytometry. The binding ability of the selected peptide to CHO-K1/VPAC1 cells and colorectal cancer (CRC) cell lines was confirmed using fluorescence microscopy and flow cytometry.

Results: A significant enrichment of phages that specifically bound to CHO-K1/VPAC1 cells was obtained after four rounds of panning. Of the selected phage clones, 16 out of 60 shared the same peptide sequence, GFRFGALHEYNS, which we termed the VP2 peptide. VP2 and vasoactive intestinal peptide (VIP) competitively bound to the VPAC1 receptor. More importantly, we confirmed that VP2 specifically bound to CHO-K1/VPAC1 cells and several CRC cell lines.

Conclusion: Our results demonstrate that the VP2 peptide could specifically bind to VPAC1 receptor and several CRC cell lines. And VP2 peptide may be a potential candidate to be developed as a useful diagnostic molecular imaging probe for early detection of CRC.

Titel:	Screening of a specific peptide binding to VPAC1 receptor from a phage display peptide library.
Autor/in / Beteiligte Person:	Tang, B ; Li, Z ; Huang, D ; Zheng, L ; Li, Q
Link:	Zum Volltext
Zeitschrift:	PloS one, Jg. 8 (2013), Heft 1, S. e54264
Veröffentlichung:	San Francisco, CA : Public Library of Science, 2013
Medientyp:	academicJournal
ISSN:	1932-6203 (electronic)
DOI:	10.1371/journal.pone.0054264
Schlagwort:	Amino Acid Sequence Animals Binding, Competitive CHO Cells Cell Line, Tumor Colorectal Neoplasms metabolism Colorectal Neoplasms pathology Cricetinae Flow Cytometry Gene Expression Humans Ligands Microscopy, Fluorescence Molecular Imaging Molecular Sequence Data Protein Binding Receptors, Vasoactive Intestinal Polypeptide, Type I genetics Sequence Analysis, DNA Transfection Vasoactive Intestinal Peptide chemistry Colorectal Neoplasms diagnosis Peptide Library Peptides genetics Peptides metabolism Receptors, Vasoactive Intestinal Polypeptide, Type I metabolism Vasoactive Intestinal Peptide metabolism
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, Non-U.S. Gov't Language: English [PLoS One] 2013; Vol. 8 (1), pp. e54264. <i>Date of Electronic Publication: </i>2013 Jan 24. MeSH Terms: Peptide Library* ; Peptides* / genetics ; Peptides* / metabolism ; Colorectal Neoplasms / diagnosis ; Receptors, Vasoactive Intestinal Polypeptide, Type I / metabolism ; Vasoactive Intestinal Peptide / *metabolism ; Amino Acid Sequence ; Animals ; Binding, Competitive ; CHO Cells ; Cell Line, Tumor ; Colorectal Neoplasms / metabolism ; Colorectal Neoplasms / pathology ; Cricetinae ; Flow Cytometry ; Gene Expression ; Humans ; Ligands ; Microscopy, Fluorescence ; Molecular Imaging ; Molecular Sequence Data ; Protein Binding ; Receptors, Vasoactive Intestinal Polypeptide, Type I / genetics ; Sequence Analysis, DNA ; Transfection ; Vasoactive Intestinal Peptide / chemistry References: Pharmacol Ther. 2009 Mar;121(3):294-316. (PMID: 19109992) ; Proc Natl Acad Sci U S A. 1993 May 15;90(10):4345-9. (PMID: 8389448) ; Peptides. 2007 Sep;28(9):1631-9. (PMID: 17574305) ; Nature. 1993 Sep 9;365(6442):170-5. (PMID: 8396727) ; World J Gastroenterol. 2012 May 7;18(17):2053-60. (PMID: 22563192) ; J Biol Chem. 1999 Nov 5;274(45):31930-40. (PMID: 10542221) ; J Nucl Med. 2011 Aug;52(8):1173-80. (PMID: 21764796) ; Appl Radiat Isot. 2007 Apr;65(4):382-6. (PMID: 17194598) ; Curr Pharm Des. 2005;11(9):1167-80. (PMID: 15853664) ; Biomaterials. 2011 Nov;32(33):8518-28. (PMID: 21880363) ; Invest New Drugs. 2008 Dec;26(6):489-504. (PMID: 18217205) ; Biopolymers. 2004;76(5):391-403. (PMID: 15389488) ; Regul Pept. 2007 Dec 4;144(1-3):101-8. (PMID: 17683807) ; Eur J Nucl Med Mol Imaging. 2004 Jun;31(6):803-10. (PMID: 14985869) ; Mol Cell Endocrinol. 2009 Apr 10;302(1):41-8. (PMID: 19101605) ; Life Sci. 2002 Jul 19;71(9):1005-14. (PMID: 12088760) ; J Biochem. 2007 Jul;142(1):79-85. (PMID: 17517791) ; Mol Biotechnol. 2012 Jul;51(3):212-20. (PMID: 21979823) ; J Biol Chem. 1996 Jan 19;271(3):1660-8. (PMID: 8576167) ; PLoS One. 2011;6(7):e22203. (PMID: 21765952) ; Cancer Res. 2000 Jun 1;60(11):3105-12. (PMID: 10850463) ; J Biol Chem. 1997 Aug 8;272(32):19666-71. (PMID: 9242621) ; Prog Neurobiol. 2009 Apr;87(4):212-51. (PMID: 19395337) ; Peptides. 2007 Sep;28(9):1655-66. (PMID: 17555844) ; Regul Pept. 2006 Nov 15;137(1-2):34-41. (PMID: 16989911) ; Cancer Lett. 2009 Aug 18;281(1):64-70. (PMID: 19327883) ; Biosci Biotechnol Biochem. 2006 Sep;70(9):2035-41. (PMID: 16960395) ; CA Cancer J Clin. 2012 Jan-Feb;62(1):10-29. (PMID: 22237781) ; Histol Histopathol. 2006 Aug;21(8):867-72. (PMID: 16691539) ; J Mol Neurosci. 2002 Feb-Apr;18(1-2):29-35. (PMID: 11931347) ; Eur J Nucl Med Mol Imaging. 2002 Jun;29(6):797-803. (PMID: 12029554) ; Chem Biol Drug Des. 2012 Mar;79(3):246-59. (PMID: 22136656) ; Gastroenterology. 2001 Feb;120(3):763-81. (PMID: 11179249) ; Regul Pept. 2004 Dec 15;123(1-3):187-92. (PMID: 15518911) ; Pharmacol Rev. 2009 Sep;61(3):283-357. (PMID: 19805477) ; J Surg Oncol. 2005 Dec 1;92(3):203-9. (PMID: 16299782) ; Peptides. 2007 Sep;28(9):1883-90. (PMID: 17580098) ; Nucl Med Biol. 2001 May;28(4):445-50. (PMID: 11395318) ; Ann N Y Acad Sci. 2006 Jul;1070:1-628. (PMID: 16991209) ; J Mol Med (Berl). 2006 Sep;84(9):764-73. (PMID: 16763842) ; Mol Cell Endocrinol. 2012 Jan 2;348(1):241-6. (PMID: 21896307) ; Br J Cancer. 1998 Jul;78(1):1-5. (PMID: 9662242) ; Ann N Y Acad Sci. 2000;921:37-44. (PMID: 11193855) ; J Biol Chem. 1998 Jul 31;273(31):19685-90. (PMID: 9677397) ; Brain Res Brain Res Rev. 2004 Aug;46(1):32-43. (PMID: 15297153) Substance Nomenclature: 0 (Ligands) ; 0 (Peptide Library) ; 0 (Peptides) ; 0 (Receptors, Vasoactive Intestinal Polypeptide, Type I) ; 0 (VIPR1 protein, human) ; 37221-79-7 (Vasoactive Intestinal Peptide) Entry Date(s): Date Created: 20130201 Date Completed: 20130708 Latest Revision: 20211021 Update Code: 20231215 PubMed Central ID: PMC3554773

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Screening of a specific peptide binding to VPAC1 receptor from a phage display peptide library.