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Biochemistry

Title:		Structure-activity relationships in the dodecapeptide alpha-factor of Saccharomyces cerevisiae: position 6 analogues are poor inducers of agglutinability
Author(s):		Baffi RA; Becker JM; Lipke PN; Naider F;
Address:
Journal Title:		Biochemistry
Year:		1985
Volume:		24
Issue:		13
Page Number:		3332 - 3337
DOI:		10.1021/bi00334a038
ISSN/ISBN:		0006-2960 (Print) 0006-2960 (Linking)
Abstract:		"Five des-Trp1,Cha3,X6 analogues of alpha-factor, where X = Ala, Val, Ile, Nle, or D-Leu and X = Leu in the natural alpha-factor sequence, were prepared by solution-phase techniques utilizing isobutyl chloroformate or 1-hydroxybenzotriazole accelerated active esters as the coupling agents. Purification to 98% or greater homogeneity was accomplished by high-performance liquid chromatography on a reversed-phase muBondapak C18 column with methanol/water/trifluoroacetic acid as the mobile phase. Three of the synthesized analogues (X6 = Val, Ile, Nle) induced morphogenesis and increased agglutinability in a cells. These substitutions demonstrate that a gamma-branched side chain at position 6 is not essential for biological activity. All of the active analogues induced morphogenesis at lower concentrations than they induced enhanced agglutinability. These results and other structure-activity relationships [Baffi, R. A., Shenbagamurthi, P., Terrance, K., Becker, J. M., Naider, F., & Lipke, P. (1984) J. Bacteriol. 158, 1152-1156] indicate that the agglutination and morphological responses to alpha-factor can be varied independently. Replacement of Leu6 with Ala or D-Leu resulted in inactive analogues that were not antagonistic for alpha-factor activity. Cell-mediated hydrolysis experiments indicated that the biological activities of the alpha-factor analogues are independent of their rates of degradation. All position 6 analogues were hydrolyzed more slowly than the parent compound, suggesting that the enzyme which degrades alpha-factor is highly specific for the native structure"
Keywords:		Agglutination Amino Acids Kinetics Mating Factor Morphogenesis/drug effects Peptides/chemical synthesis/*pharmacology/physiology Saccharomyces cerevisiae/drug effects/*physiology Structure-Activity Relationship;
Notes:		"MedlineBaffi, R A Becker, J M Lipke, P N Naider, F eng GM 22086/GM/NIGMS NIH HHS/ GM 22087/GM/NIGMS NIH HHS/ Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. 1985/06/18 Biochemistry. 1985 Jun 18; 24(13):3332-7. doi: 10.1021/bi00334a038"