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Title 

Stronger anti-HIV-1 activity of C-peptide derived from HIV-I89.6 gp41 C-terminal heptad repeated sequence

 

인간면역바이러스 89.6형에서 유래한 C-peptide의 강한 항 인간면역바이러스 활성

Authors 

Jeong Kon SeoHee Kyung KimTae Young LeeK S HahmK L KimMyung Kyu Lee

Publisher 

Elsevier

Issue Date 

2005

Citation 

Peptides, vol. 26, no. 11, pp. 2175-2181

Keywords 

anti-HIV-1 assayanti-HIV-1 peptideC-peptide of HIV-1 gp41HIV-189.6 strainamino terminal sequencecarboxy terminal sequenceamino acid sequencemolecular sequence data

Abstract 

C34-LAI containing amino acids 118 to 151 of the HIV-1LAI gp41 ectodomain exhibits potent anti-HIV-1 activity. However, the N-terminal halves of C34 peptides vary more according to the HIV-1 strain than the C-terminal halves. Therefore, an analysis was conducted on the anti-HIV-1 activities of the C34 peptides derived from various HIV-1 strains. C34-89.6 exhibited the strongest anti-HIV-1 activity among the C34 peptides tested. Interestingly, its N-terminal half was more acidic than those of the other C34 peptides, whereas its C-terminal half was more basic. Since the C-peptides derived from the HIV-1LAI strain are used extensively, the anti-HIV-1 activities of these peptides were compared between the HIV-1 strains 89.6 and LAI. When using chimeric peptides, it was found that the C-terminal basic region of C34-89.6 was more critical than its N-terminal basic region. The anti-HIV-1 activity of T20-89.6 and C28-89.6 was also stronger than that of T20-LAI and C28-LAI, respectively. The anti-HIV-1 activity of C28-89.6 was weakened when the C-terminal basic residues were changed to the corresponding residues of C28-LAI. However, no conformational differences were found among the C28 peptides. Accordingly, these results imply that introducing the C-terminal basic residues of the HIV-189.6 C-peptide may be useful for developing potent anti-HIV-1 drugs.

ISSN 

0196-9781

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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