Bitterness of Peptides: Amino Acid Composition and Chain Length

作者：KARL HEINZ NEY · 发表于：ACS symposium series · 年份：1979 · DOI：10.1021/bk-1979-0115.ch006 · 被引用次数：147 · 研究领域：Protein Structure and Dynamics、Machine Learning in Bioinformatics、Chemical Synthesis and Analysis

During our work on taste of foods we synthesized a series of peptides and soon came to the opinion, that the bitterness of peptides is caused by the hydrophobic action of amino acid side chains. Here I think some remarks on hydrophobic interactions ( 1 ) would be appropriate. It is generally accepted now, that hydrophobic interactions are a contributing factor to protein behaviour and esp. to the formation of the secondary structure, e.g. helix. This means, that as shown in Figure 1 hydrophobic residues of the amino acids in a peptide are driven together by clusters of water molecules and so the secondary structure of a peptide or protein is formed. For the transfer from the helical to the stretched form, Tanford ( 2 ) found that the transfer free energy of the total protein results from the sum of the contributions of the single amino acid residues. The Δf values of the