Abstract
In spite of the relevance of the results obtained through the clinical application of chemotherapeutic agents (reverse transcriptase and proteinase inhibitors) that are able to prolong the life span of affected people, acquired immunodeficiency syndrome (AIDS) remains a serious and lethal disease. AIDS is caused by a type 1 human immunodeficiency virus (HIV-1) and formation of a complex among the gp120, CD4 and CCR5 / CXCR4 surface proteins represents a key-step in the infection. The use of synthetic peptides reproducing reduced sequences of these proteins has contributed to increase the knowledge of the mechanism that determines the penetration of the HIV viruses into the targetcells. In addition, short peptides with minimum structural requirements for anti-HIV activity hold greater potential as lead compounds for rational drug design than macromolecular proteins. In this context, our studies concern: the role of gp120 V3 loop in CD4 binding, the importance of the N-terminal sequence of HIV CCR5 coreceptor, the potential inhibitory properties of sequences patterned on CXCR4 natural ligand (SDF-1) and the role of secondary structure in determining gp160 enzymatic processing into gp120.
Related Journals
Protein & Peptide Letters
Related Books
Frontiers in Protein and Peptide Sciences
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