Linked Life Data

9230468

Source:http://linkedlifedata.com/resource/pubmed/id/9230468

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-8-27
pubmed:abstractText
A series of peptides patterned on the principal neutralizing domain of the HIV-1 envelope glycoprotein gp 120 have been synthesized by solid-phase techniques. Interestingly, in vitro experiments have shown that some of these peptides specifically interact with CD4 and, in particular, that the peptide corresponding to the sequence 307-330 of the HIV-1 MN isolate was able to enhance infection in a dose-specific and not a strain-restricted way. To bypass problems observed in preliminary runs, peptides were synthesized by both Fmoc and Boc chemistry. Comparison of the two strategies has allowed the set up of convenient protocols for the preparation of the target peptides in good yield, and with the high-purity grade needed for biological and physiochemical studies. Since the biological effects were present in the carboxyl-free C-terminal linear peptide but not in the amidated C-terminal analogue, preliminary conformational studies by circular dichroism and nuclear magnetic resonance techniques were also performed in an attempt to correlate these effects with possible contributions of structured conformations as predicted by theoretical calculations. The possibility of a beta-turn structure for the crucial Gly-Pro-Gly-Arg sequence has been confirmed by 2D NMR experiments. Ongoing studies suggest the exploitation of the activating properties of the MN-derived peptides to design a more sensitive and innovative serological test based on the virus itself and not on anti-HIV antibodies, as is the case for the large majority of tests currently in use.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1075-2617
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Synthesis, characterization and conformational analysis of gp 120-derived synthetic peptides that specifically enhance HIV-1 infectivity.
pubmed:affiliation
Institute for Industrial Chemistry, University of Padua, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't