Conformational properties of N-acetyl-N-methyl-alpha,beta-dehydroalanine N'-methylamide

• Autorzy: Macedowska A. , Siodlak D. , Rzeszotarska B.
• Języki publikacji: EN

Abstrakty

EN

The conformational properties of Ac-Δ(Me)Ala-NHMe (N-acetyl-N-methyl-α,β-dehydroalanine N'-methylamide), as the simplest model of N-methyl-α,β-dehydroamino acids, was examined with theoretical methods and in comparison with Ac-ΔAla-NHMe and Ac-ΔAla-NMe2. The N-terminal amide of the Δ(Me)Ala residue easily adopts the configuration cis and the torsion angles φ, ψ are highly flexible. The Δ(Me)Ala residue is a conformational flexibilizer as compared to the parent ΔAla, which is a conformational stiffener. This seems to be the reason why Δ(Me)Ala is found in small natural cyclic peptides, where it ensures the conformational flexibility necessary for biological action.

Słowa kluczowe

EN

N-acetyl-N-methyl-alpha,beta-dehydroalanine N'-methylamide; cis-trans isomerization; N-alkylpeptide; beta-dehydroamino acid; peptide design; alpha-dehydroamino acid

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2006
• Tom: 53
• Numer: 1
• Opis fizyczny: p.227-232,fig.,ref.

Twórcy

autor

Macedowska A.

• University of Opole, Opole, Poland

autor

Siodlak D.

autor

Rzeszotarska B.

Bibliografia

• Allen FH, Baalham CA, Lommerse JPM, Raithby PR (1998) Acta Cryst B: 54: 320–329.
• Bágyi I et al. (2003) J Mol Struct (Theochem) 625: 121–136.
• Ballard CE, Yu H, Wang B (2002) Curr Med Chem 9: 471–498.
• Broda MA, Rzeszotarska B, Smełka L, Pietrzyński G (1998) J Peptide Res 52: 72–79.
• Broda MA, Siodłak D, Rzeszotarska B (2005a) J Peptide Sci 11: 235–244.
• Broda MA, Siodłak D, Rzeszotarska B (2005b) J Peptide Sci 11: 546–555.
• Dawson RM (1998) Toxicon 36: 953–962.
• Frisch MJ et al. (2003) Gaussian 03, Revision B.04, Gaussian, Inc., Pittsburgh, PA, 2003.
• Gilon C, Dechantstreiter MA, Burkhart F, Friedler A, Kessler H (2002) Methods of Organic Chemistry (Houben-Weyl) vol. E22c, p 215, Georg Thieme Verlag, Stuttgart.
• Head-Gordon T, Head-Gordon M, Frisch MJ, Brooks III ChL, Pople JA (1991) J Am Chem Soc 113: 5989–5997.
• Herzberg O, Moult J (1991) Proteins 11: 223–229.
• Loiseau N, Cavelier F, Noel J-P, Gomis J-N (2002) J Peptide Sci 8: 335–346.
• Łukomska J, Kasprzykowski F, Łankiewicz L, Grzonka Z (2002) Wiad chem 56: 57–82.
• Miertus S, Scrocco E, Tomasi J (1981) Chem Phys 55: 117–129.
• Miyamae A, Fujioka M, Koda S, Morimoto Y (1989) J Chem Soc Perkin Trans I 873–878.
• Proksch P, Edrada RA, Ebel R (2002) Appl Microbiol Biotechnol 59: 125–134.
• Ramachandran GN, Sasisekharan V (1968) Adv Protein Chem 23: 283–438.
• Siodłak D, Broda MA, Rzeszotarska B (2004a) J Mol Struct (Theochem) 668: 75–85.
• Siodłak D, Rzeszotarska B, Broda MA, Kozioł AE, Kołodziejczyk E (2004b) Acta Biochim Polon 51: 145–152.
• Sivonen K, Namikoshi M, Evans WR, Carmichael WW, Sun F, Rouhiainen L, Luukkainen L, Reinahrt KL (1992) Appl Envir Microbiol 58: 2495–2500.
• Steiner T (2002) Angew Chem Int Ed Engl 41: 48–76. Surfer 8. Golden Software, Inc. 2002.
• Thormann M, Hofmann H-J (1998) J Mol Struct (Theochem) 431: 79–96.
• Zimmerman SS, Pottle MS, Némethy G, Scheraga HA (1977) Macromolecules 10: 1–9.