Linked Life Data

11311058

Source:http://linkedlifedata.com/resource/pubmed/id/11311058

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2001-4-20
pubmed:abstractText
To identify novel peptides that inhibit the interaction between human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp120 and CD4, we constructed a targeted phage-displayed peptide library in which phenylalanine and proline were fixed at the fourth and sixth positions, respectively, because Phe43 and the adjacent beta-turn of CD4 are critical for interaction with gp120. Two synthetic peptides were selected after three rounds of biopanning against gp120, and one of them, G1 peptide (ARQPSFDLQCGF), exhibited specific inhibition of the interaction between gp120 and CD4 with an IC(50) of about 50 microM. Structural analysis using NMR demonstrated that G1 peptide forms a compact cyclic structure similar to the CD4 region interacting with gp120. Two derivatives of G1 peptide, a linear hexameric peptide (G1-6) and a cyclic nonameric peptide (G1-c), were synthesized based on the structure of the G1 peptide. Interestingly, they showed higher inhibitory activities than did G1 peptide with IC(50)'s of 6 and 1 microM, respectively. Thus, this study might provide a new insight into the development of anti-HIV-1 inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2623
pubmed:author
pubmed:issnType
Print
pubmed:day
26
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1356-63
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Short peptides with induced beta-turn inhibit the interaction between HIV-1 gp120 and CD4.
pubmed:affiliation
Department of Molecular Life Science, Pohang University of Science and Technology, Pohang, Kyungbuk, Republic of Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't