A novel specific small molecule peptide for small cell lung cancer

Lin Lang Guo, Ying Quo, Derick H Lau, Sha Xiao, Yin Chao Xu, Hong Shen

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Screen small molecule peptide specific binding to small cell lung cancer cell (DMS53) was screened by using the "one-bead one-peptide" combinatorial technology. Thirty two positive beads binding to DMS53 were totally obtained after primary screening. Consensus peptide sequences of cXNGRXXc and cNGRXXXc were identified by amino acid sequencing in ten beads. Three representative peptides were re-synthesized on beads. Secondary screening showed that cell adhesion percentage of cFNGRQQc to DMSS was higher than the other two peptides. cFNGRQQc was further studied for cell specificity, alanine scanning and site-directed deletion. The results showed that cFNGRQQc is specific for promoting cell adhesion to DMS53 but not to other human cell lines. Both motif of -NGR- and the length of six peptide of cFNGRQQc structure are important for DMS53 attachment, In an antibody or peptide blocking assay, cell adhesion of DMS53 to peptide bead was not inhibited by antibodies or peptides including anti-integrin, E-cadherin, NCAM and ICAM. The binding site on DMS53 surface for cFNGRQQc peptide need to be proven in the future.

Original languageEnglish (US)
Pages (from-to)562-566
Number of pages5
JournalProgress in Biochemistry and Biophysics
Volume33
Issue number6
StatePublished - Jun 2006

Fingerprint

Small Cell Lung Carcinoma
Cells
Peptides
Molecules
Cell adhesion
Cell Adhesion
Screening
Neural Cell Adhesion Molecules
Antibodies
Protein Sequence Analysis
Consensus Sequence
Cadherins
Integrins
Alanine
Assays
Binding Sites
Technology
Scanning
Amino Acids
Cell Line

Keywords

  • Combinatorial chemistry
  • Small cell lung cancer
  • Small molecule peptide

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

Cite this

Guo, L. L., Quo, Y., Lau, D. H., Xiao, S., Xu, Y. C., & Shen, H. (2006). A novel specific small molecule peptide for small cell lung cancer. Progress in Biochemistry and Biophysics, 33(6), 562-566.

A novel specific small molecule peptide for small cell lung cancer. / Guo, Lin Lang; Quo, Ying; Lau, Derick H; Xiao, Sha; Xu, Yin Chao; Shen, Hong.

In: Progress in Biochemistry and Biophysics, Vol. 33, No. 6, 06.2006, p. 562-566.

Research output: Contribution to journalArticle

Guo, LL, Quo, Y, Lau, DH, Xiao, S, Xu, YC & Shen, H 2006, 'A novel specific small molecule peptide for small cell lung cancer', Progress in Biochemistry and Biophysics, vol. 33, no. 6, pp. 562-566.
Guo, Lin Lang ; Quo, Ying ; Lau, Derick H ; Xiao, Sha ; Xu, Yin Chao ; Shen, Hong. / A novel specific small molecule peptide for small cell lung cancer. In: Progress in Biochemistry and Biophysics. 2006 ; Vol. 33, No. 6. pp. 562-566.
@article{38156ee29411418ea207ba8a9a515626,
title = "A novel specific small molecule peptide for small cell lung cancer",
abstract = "Screen small molecule peptide specific binding to small cell lung cancer cell (DMS53) was screened by using the {"}one-bead one-peptide{"} combinatorial technology. Thirty two positive beads binding to DMS53 were totally obtained after primary screening. Consensus peptide sequences of cXNGRXXc and cNGRXXXc were identified by amino acid sequencing in ten beads. Three representative peptides were re-synthesized on beads. Secondary screening showed that cell adhesion percentage of cFNGRQQc to DMSS was higher than the other two peptides. cFNGRQQc was further studied for cell specificity, alanine scanning and site-directed deletion. The results showed that cFNGRQQc is specific for promoting cell adhesion to DMS53 but not to other human cell lines. Both motif of -NGR- and the length of six peptide of cFNGRQQc structure are important for DMS53 attachment, In an antibody or peptide blocking assay, cell adhesion of DMS53 to peptide bead was not inhibited by antibodies or peptides including anti-integrin, E-cadherin, NCAM and ICAM. The binding site on DMS53 surface for cFNGRQQc peptide need to be proven in the future.",
keywords = "Combinatorial chemistry, Small cell lung cancer, Small molecule peptide",
author = "Guo, {Lin Lang} and Ying Quo and Lau, {Derick H} and Sha Xiao and Xu, {Yin Chao} and Hong Shen",
year = "2006",
month = "6",
language = "English (US)",
volume = "33",
pages = "562--566",
journal = "Progress in Biochemistry and Biophysics",
issn = "1000-3282",
publisher = "Science Press",
number = "6",

}

TY - JOUR

T1 - A novel specific small molecule peptide for small cell lung cancer

AU - Guo, Lin Lang

AU - Quo, Ying

AU - Lau, Derick H

AU - Xiao, Sha

AU - Xu, Yin Chao

AU - Shen, Hong

PY - 2006/6

Y1 - 2006/6

N2 - Screen small molecule peptide specific binding to small cell lung cancer cell (DMS53) was screened by using the "one-bead one-peptide" combinatorial technology. Thirty two positive beads binding to DMS53 were totally obtained after primary screening. Consensus peptide sequences of cXNGRXXc and cNGRXXXc were identified by amino acid sequencing in ten beads. Three representative peptides were re-synthesized on beads. Secondary screening showed that cell adhesion percentage of cFNGRQQc to DMSS was higher than the other two peptides. cFNGRQQc was further studied for cell specificity, alanine scanning and site-directed deletion. The results showed that cFNGRQQc is specific for promoting cell adhesion to DMS53 but not to other human cell lines. Both motif of -NGR- and the length of six peptide of cFNGRQQc structure are important for DMS53 attachment, In an antibody or peptide blocking assay, cell adhesion of DMS53 to peptide bead was not inhibited by antibodies or peptides including anti-integrin, E-cadherin, NCAM and ICAM. The binding site on DMS53 surface for cFNGRQQc peptide need to be proven in the future.

AB - Screen small molecule peptide specific binding to small cell lung cancer cell (DMS53) was screened by using the "one-bead one-peptide" combinatorial technology. Thirty two positive beads binding to DMS53 were totally obtained after primary screening. Consensus peptide sequences of cXNGRXXc and cNGRXXXc were identified by amino acid sequencing in ten beads. Three representative peptides were re-synthesized on beads. Secondary screening showed that cell adhesion percentage of cFNGRQQc to DMSS was higher than the other two peptides. cFNGRQQc was further studied for cell specificity, alanine scanning and site-directed deletion. The results showed that cFNGRQQc is specific for promoting cell adhesion to DMS53 but not to other human cell lines. Both motif of -NGR- and the length of six peptide of cFNGRQQc structure are important for DMS53 attachment, In an antibody or peptide blocking assay, cell adhesion of DMS53 to peptide bead was not inhibited by antibodies or peptides including anti-integrin, E-cadherin, NCAM and ICAM. The binding site on DMS53 surface for cFNGRQQc peptide need to be proven in the future.

KW - Combinatorial chemistry

KW - Small cell lung cancer

KW - Small molecule peptide

UR - http://www.scopus.com/inward/record.url?scp=33749179227&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33749179227&partnerID=8YFLogxK

M3 - Article

AN - SCOPUS:33749179227

VL - 33

SP - 562

EP - 566

JO - Progress in Biochemistry and Biophysics

JF - Progress in Biochemistry and Biophysics

SN - 1000-3282

IS - 6

ER -