Synthesis and biological activity of acylated and telomerized peptides as potential HIV-fixation inhibitors.
In order to inhibit the gp 120-CD4 glycoprotein interaction, a key step of the HIV-infection, we have synthesized a series of N-acylated peptides containing sequences identified in both the viral and lymphocytic proteins, (SDFR, SDAR, RFDSAARFDS, DRADSRRS, PSKLNDRADSRRSLWD, ASTTTNYT). An hydrophobic moiety (capryloyl, palmitoyl acrylamidoundecanoyl) was introduced in the last step of interactive synthesis, in homogeneous or solid phase. The acrylogyl-containing compounds were then telomerized under UV irradiation (DPn observed: 2 to 6). The biological evaluation shown an antiviral effect in vitro for telomerized peptides containing amino diacids such as Glu and Asp.
Lacoux
X
X
Laboratoires de Chimie Biomoléculaire, Université de Montpellier-II, France.
Barragan
V
V
Dewynter
G
G
Leydet
A
A
Roque
J P
JP
Montero
J L
JL
D000215:Acylation; D000595:Amino Acid Sequence; D019380:Anti-HIV Agents / Q000138:chemical synthesis* / Q000494:pharmacology; D016860:CD4 Immunoadhesins / Q000378:metabolism; D015699:HIV Envelope Protein gp120 / Q000378:metabolism; D015497:HIV-1 / Q000187:drug effects; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis* / Q000494:pharmacology; D013237:Stereoisomerism
D019380:Anti-HIV Agents; D016860:CD4 Immunoadhesins; D015699:HIV Envelope Protein gp120; D010455:Peptides