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- Title
Highly Active Analogs of α-Factor and Their Activities Against Saccharomyces cerevisiae.
- Authors
Hee Jun Ahn; Eun Young Hong; Dong Hoon Jin; Nam Joo Hong
- Abstract
Thirteen analogs of tridecapeptide α-factor (WHWLQLKPGQPMY) of Saccharomyces cerevisiae with C- or N-terminal Trp extension and isosteric replacement by Aib at position 8 and 11, Trp at position 13, D-Ala at position 9, and Orn and Glu at position 6 were synthesized and assayed for their biological activity. Receptor binding assay was carried out using our newly developed spectrophotometric method with detector peptide 14. C- or N-terminal extended analogs, α-factor-[Trp]n (n =1-5) 1-5 and [N-Trp]1-α-factor 6, were all less active than native α-factor and gradual decreases in both activity and receptor affinity were observed with greater Trp extension. Trp-substituted analog at position 13, [Trp13]α-factor 7, exhibited about 2-fold reductions in both activity and receptor affinity. Aib-substituted analogs, [Aib8]α-factor 8 and [Aib11]α-factor 9, showed 5- to 10-fold reduction in activity as well as 3-fold reduction in receptor affinity compared to native α-factor. [Orn6]α-factor 10 demonstrated strong potency with a 7.0-fold increase in halo activity as well as 1.8-fold increase in receptor affinity compared to native α-factor. For two double substituted analogs, [Glu6,D-Ala9]α-factor 12 showed the slightly decreased potency in halo activity compared to analog 10, whereas [Orn6,D-Ala9]α-factor 11 exhibited 15-fold higher halo activity as well as nearly 3-fold higher receptor affinity compared to native α-factor.
- Subjects
SACCHAROMYCES cerevisiae; SACCHAROMYCES; BINDING site assay; SPECTROPHOTOMETRY; PEPTIDES
- Publication
Bulletin of the Korean Chemical Society, 2014, Vol 35, Issue 5, p1365
- ISSN
0253-2964
- Publication type
Article
- DOI
10.5012/bkcs.2014.35.5.1365