Quantitative Analyses of Hydrophobicity of Di- to Pentapeptides Having Un-ionizable Side Chains with Substituent and Structural Parameters

Akamatsu, Miki; Fujita, Toshio

doi:10.1002/jps.2600810213

Cited by 40 publications

(33 citation statements)

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“…For peptides higher than tripeptides, variations in the log P(O/W) are also governed by the ease of intramolecular transannular hydrogen-bond formation leading to /?-turns and a-helices. 26 The increment attributable t o the /?-turn formation in linear tetra-and pentapeptides has been analyzedz6 by considering an equilibrium between "random" and /?-turned conformations using the equilibrium constant defined by the Chou-Fassman p-turn propensity parameter^.^^ In the octanol phase, the @-turned conformation is predominant. In the water phase, however, "random" structures are preferred.…”

Section: Discussionmentioning

confidence: 99%

Quantitative Structure-Hydrophobicity and Structure-Activity Relationships of Antibacterial Gramicidin S Analogs

Katayama

Nakao

Akamatsu

et al. 1994

Journal of Pharmaceutical Sciences

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Section: Discussionmentioning

confidence: 99%

Quantitative Structure-Hydrophobicity and Structure-Activity Relationships of Antibacterial Gramicidin S Analogs

Katayama

Nakao

Akamatsu

et al. 1994

Journal of Pharmaceutical Sciences

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“…The isoelectric points of the tested dipeptides seerned to range between pH 5.2-5.7 (Akamatsu & Fujita, 1992). Because the charge of each peptide depends on pH, its adsorbability might be affected by pH.…”

Section: Resultsmentioning

confidence: 99%

“…The logarithm of the partition ratio (logP') in l-octanol-aqueous system is a measure of peptide hydrophobicity. An empirical equation correlating logP' of a peptide at pH 7 to the sum of the hydrophobic parameter of the side chain substituents ~7r and the corrected Dubois steric parameter Es" has been reported (Akamatsu & Fujita, 1992). The logP' values ofthe tested peptides were evaluated using this equation and are shown in Table I .…”

Section: Discussionmentioning

confidence: 99%

“…The volume of adsorbate qm,cal [moVkg] o E (3) and (4) with those experimentally observed at pH 7. ~)logP'=0.943~;r+0.550Es"(RN)+0.307Es"(Rc)+0'1351Y+0.375lw+0'6541M+1.584ls~3'838 where IY, Iw, IM and Is are indicator depending on the absence or presence, respectively, of tyrosine, tryptophan, methionine, and serine (Akamatsu & Fujita, 1992).…”

Section: Discussionmentioning

confidence: 99%

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Adsorption of Dipeptides on Activated Carbon.

Adachi

Yamanaka

Matsuno

1998

FSTI

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The adsorption isotherms of some dipeptides composed of un-ionizable side chains were measured at 25'C in a single component system, and all of them obeyed the Langnnuir equation. The parameters obtained at pH 7 could be roughly correlated with the hydrophobic and steric parameters of constituent amino acids. To find a method for predicting the amount of dipeptide adsorbed under various conditions, the applicability of the Polanyi adsorption potential theory was examined. The amount of dipeptide adsorbed could be roughly estimated from the adsorption isotherms of the amino acids, although the estimation lacked strictness in a physical sense.Keywords: adsorption, dipeptide, activated carbon Attention has been paid to the utilization of protein hydrolysate as a food seasoning (Ueno et at, 1990) and foaming agent (Nagatomo et al, 1990). In these applications, a separation process is incorporated to obtain a peptide mixture with a specific functionality. An infusion solution rich in branched amino acids and poor in aromatic ones is useful as a nutrient for patients with liver diseases (Fischer et al, 1976). A peptide mixture with such an amino acid composition would be more promising than an amino acid mixture because of its faster absorption in the intestine and lower osmotic pressure. We reported the preparation of a peptide mixture with a high Fischer ratio, which is the ratio of branched amino acids to aromatic ones, from the enzymatic hydrolysate of casein using gel chromatographic resin (Adachi et al, 1991) or activated carbon (Adachi et al, 1993). The preparation of a peptide mixture rich in aromatic amino acids from a protein hydrolysate was also attempted (Li et al, 1985). Thus, peptides with a definite composition would be useful as foodstuffs.To reasonably design an adsorptive separation of peptides, knowledge of their adsorption equilibria and rate processes is required. A protein hydrolysate includes many kinds of peptides. It would be difficult to predict the adsorption isotherm of each peptide onto an adsorbent in a multi-component system. As the first step in the adsorptive separation design of peptides from protein hydrolysate, we measured the adsorption isotherms of some dipeptides composed of amino acids having un-ionizable side chains onto an activated carbon in a single component system, and the methods to predict them are discussed. Materials and MethodsMaterials Glycyl-L-isoleucine (Gly-Ile), glycyl-L-leucine (Gly-Leu), glycyl-L-phenylalanine (Gly-Phe), glycyl-L-tryptophan (Gly-Trp), glycyl-L-tyrosine (Gly-Tyr), L-leucyl-L-leucine (Leu-Leu), L-leucyl-L-tyrosine (Leu-Tyr) and L-phenylalanyl-L-leucine (Phe-Leu) were purchased from Sigma(Ser-Leu) were obtained from Kokusan Chemical Works, Osaka. Glycylglycine (Gly-Gly) and most ofthe amino acids used were purchased from Wako Pure Chemical Industries, Osaka. L-Tryptophan and L-tyrosine were products of the Peptide Institute, Osaka. Other chemicals were purchased from Nacalai Tesque or Wako Pure Chemical Industries and were of analytical grade.Th...

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“…Numerous methods are available for calculating hydrophobic parameters [4,8,12,14,[52][53][54][55][56][57][58][59][60][61][62][63][64][65][66][67][68], but many of these do not utilize three-dimensional structures. However, some methods do employ three-dimensional structures in the calculation [69-711 .…”

Section: Partition Coefficients (Log P) Of Furan Analogsmentioning

confidence: 99%

Calculation of hydrophobic parameters directly from three-dimensional structures using comparative molecular field analysis

Kim

1995

J Computer-Aided Mol Des

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Capacity ratio (log k') values, which are a measure of hydrophobicity, were calculated directly from the three-dimensional structures of 17 furans and 54 triazines using the comparative molecular field analysis approach. The H2O probe and the GRID force field, including hydrogen-bond potentials, yielded excellent correlations with the log k' values. Moreover, the predicted values of log k' from 14 additional triazine analogs showed excellent agreement with log k' values reported in the literature. Similar results were obtained for the octanol-water partition coefficients (log P) of 17 furans.

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Quantitative Analyses of Hydrophobicity of Di- to Pentapeptides Having Un-ionizable Side Chains with Substituent and Structural Parameters

Cited by 40 publications

References 28 publications

Quantitative Structure-Hydrophobicity and Structure-Activity Relationships of Antibacterial Gramicidin S Analogs

Quantitative Structure-Hydrophobicity and Structure-Activity Relationships of Antibacterial Gramicidin S Analogs

Adsorption of Dipeptides on Activated Carbon.

Calculation of hydrophobic parameters directly from three-dimensional structures using comparative molecular field analysis

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