Accession Number:

ADA230342

Title:

Molecular Recognition of Alpha-Neurotoxins

Descriptive Note:

Midterm rept. 15 Mar 1989-14 Sep 1990

Corporate Author:

BAYLOR COLL OF MEDICINE HOUSTON TX

Personal Author(s):

• Atassi, Zouhair M.

Report Date:

1990-11-30

Pagination or Media Count:

27.0

Abstract:

Synthesis, purification and characterization of the human AcChoR alpha-chain peptides have been reported 10. The alpha-neurotoxin binding regions on human AcChoR reside in the peptides shown in Fig. 1. These peptides were employed in the present work. The receptor-binding regions on Bgt are present in the three loop peptides. The synthesis, purification and characterization of the monomeric forms of the three cyclic peptidesFig. 1. have been described. Bgt and its synthetic peptides were labeled with iodine-125 using the chloramine-T method. Radioiodinated materials were used immediately after labeling. The specific activities of the labeled peptides were LIN,3. 1x103 cpmp mole L2, 2.4x103cpmp mole L3E, 2.1x103cpmp mole. The coupling of proteins and peptides to CNBr-activated Sepharose CL-4B was carried out under optimum conditions as described previously. The binding of I-labeled Bgt or Bgt peptides to adsorbents of the human AcChoR peptides was determined by a quantitative solid-phase radiometric binding assay.

Descriptors:

• *PEPTIDES
• OPTIMIZATION
• SYNTHESIS
• SOLID PHASES
• PURIFICATION
• LOOPS
• ADSORBENTS
• COUPLING(INTERACTION)
• PROTEINS

Subject Categories:

• Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE