Inhibition of oligopeptide transport in S. cerevisiae by a peptide-poly (ethylene glycol) conjugate

Naider, Fred; Khan, Sundas; Parker, David D.; Becker, Jeffrey M.

doi:10.1016/0006-291x(80)91598-3

Cited by 2 publications

(1 citation statement)

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“…On the basis of the present study, however, it is not possible to conclude whether the effect of PEGM is due to the chemical modification of the carboxyl terminus or the size of the macromolecular protecting group. Previous studies have shown that biotin conjugated to ferritin inhibited biotin uptake into yeast sphaeroplasts (Bayer et al, 1978) and trimethionine attached to polyethylene oxide) competed with (Met)3 transport into S. cerevisiae (Naider et al, 1980).…”

Section: Discussionmentioning

confidence: 98%

Structure-activity relationships in the dodecapeptide .alpha. factor of Saccharomyces cerevisiae

Shenbagamurthi¹,

Baffi²,

Khan³

et al. 1983

Biochemistry

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Ten analogues of His-Trp-Leu-Gln-Leu-Lys-Pro-Gly-Gln-Pro-Met-Tyr, the dodecapeptide alpha factor of Saccharomyces cerevisiae, were synthesized by conventional solution phase techniques and purified by using high-performance liquid chromatography. The dodecapeptide was also synthesized attached at its carboxyl terminus to poly(ethylene oxide), a macromolecular protecting group. Analogues in which Lys6 or His1 was modified exhibited high biological activity as evidenced by their ability to elicit aberrant morphologies in a cells of S. cerevisiae. These results suggest that neither a free alpha-amine nor a protonatable side chain at position 6 is necessary for biological activity of the dodecapeptide alpha factor. Although Ala2- and Phe2-dodecapeptides were not biologically active, they competed with the natural alpha factor and several active analogues. Thus binding of the alpha factor is not sufficient to elicit a biological response; it appears that the side chain in position 2 is critical for triggering morphological alterations in a cells.

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Section: Discussionmentioning

confidence: 98%