Document Detail

Anion Transport in Liposomes Responds to Variations in the Anchor Chains and the Fourth Amino Acid of Heptapeptide Ion Channels.
MedLine Citation:
PMID:  19169373     Owner:  NLM     Status:  Publisher    
Seven heptapeptide derivatives have been prepared. The peptide structure is (Gly)(3)Xxx(Gly)(3) in which Xxx stands for a variable amino acid. The amino acid variations include azetidine carboxylic acid, pipecolic acid, meta-aminobenzoic acid, proline, and leucine. All seven compounds have a C-terminal benzyl group. In all cases, the heptapeptide's N-terminus was linked to diglycolic acid and a dialkylamine. In five cases, the N-terminal group was didecylamine and in two cases, N-ethyl-N-decyl. Chloride and carboxyfluorescein release from phospholipid vesicles was studied with the result that C(10)H(21)N(C(2)H(5)) COCH(2)OCH(2)CO-NH-(Gly)(3)Leu(Gly)(3)-OCH(2)Ph was the most active. Hill analysis showed that this compound involves pore formation by four monomer units rather than two, as previously found for other members of this family.
Riccardo Ferdani; Robert Pajewski; Natasha Djedovič; Jolanta Pajewska; Paul H Schlesinger; George W Gokel
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Publication Detail:
Journal Detail:
Title:  New journal of chemistry = Nouveau journal de chimie     Volume:  29     ISSN:  1144-0546     ISO Abbreviation:  New J Chem     Publication Date:  2005  
Date Detail:
Created Date:  2009-3-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8709755     Medline TA:  New J Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  673-280     Citation Subset:  -    
Department of Molecular Biology & Pharmacology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8103, St. Louis, MO 63110 USA.
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MeSH Terms
Grant Support
R01 GM063190-04S1//NIGMS NIH HHS

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