Scientific article

Structure-Lipophilicity and Structure-Polarity Relationships of Amino-Acids and Peptides

Published inHelvetica chimica acta, vol. 78, no. 2, p. 471-485
Publication date1995

The objectives of this study were to gain insights into the structure-lipophilicity relationships of peptides and to propose an improved model for estimating their lipophilicity. First, existing databases were extended to obtain the distribution coefficients of a total of 208 free or protected peptides (di- to pentapeptides). The polarity parameters (Lambda) of 23 free amino acids and 19 protected amino acids (AcNH-CHR-CONH2) and of their side chains were calculated from experimental distribution coefficients and computed molecular volumes. An analysis of the polarity parameters revealed that the hydrophobicity of the amino-acid side chains is largely reduced due to the polar field of the backbone. The polarity parameters of the peptides were then obtained in a similar manner and shown to be highly correlated with the sum of the polarity parameters of their side chains, i.e., the lipophilicity of peptides can be calculated from their molecular volume and the sum of their side-chain polarities using the regression established for each individual series of peptides (Fig. 1). This last restriction is essential since the polarity and lipophilic increment of a NH-C*H-CO unit were shown to decrease with increasing length of backbone

Affiliation Not a UNIGE publication
Citation (ISO format)
VALLAT, P. et al. Structure-Lipophilicity and Structure-Polarity Relationships of Amino-Acids and Peptides. In: Helvetica chimica acta, 1995, vol. 78, n° 2, p. 471–485.
  • PID : unige:10001
ISSN of the journal0018-019X

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