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Blocking of CD4 cell receptors for the human immunodeficiency virus type 1 (HIV-1) by chemically modified bovine milk proteins: potential for AIDS prophylaxis.
Neurath AR; Debnath AK; Strick N; Li YY; Lin K; Jiang S; Laboratory of
August 30, 1996
J Mol Recognit. 1995 Sep-Oct;8(5):304-16. Unique Identifier : AIDSLINE

The chemical transformation of synthetic combinatorial libraries to increase the diversity of compounds of medicinal interest was reported recently. Chemical modification of natural products represents a complementary approach to accomplish this aim. Modification of lysines by aromatic acid anhydrides, preferentially by 3-hydroxyphthalic and trimellitic anhydrides and trimellitic anhydride chloride, converted commonly available proteins (human and bovine serum albumin and casein) into potent inhibitors of (i) binding between the HIV-1 gp 120 envelope glycoprotein and the CD4 cell receptor, probably owing to their binding to CD4, and (ii) infection by HIV-1. Modified bovine milk proteins are also potent HIV-1 inhibitors and may have potential for anti-HIV-1 prophylaxis.

Anhydrides Animal Antibodies, Monoclonal Antigens, CD4/*CHEMISTRY/*DRUG EFFECTS/PHYSIOLOGY Antiviral Agents/*PHARMACOLOGY Arginine Cattle CD4-Positive T-Lymphocytes/*IMMUNOLOGY/VIROLOGY Female Human HIV/*PHYSIOLOGY Lysine Milk Proteins/*PHARMACOLOGY Models, Molecular Molecular Structure *Protein Conformation Serum Albumin, Bovine/PHARMACOLOGY Structure-Activity Relationship Support, Non-U.S. Gov't Support, U.S. Gov't, P.H.S. JOURNAL ARTICLE