First application of the Dakin-West reaction to fmoc chemistry: Synthesis of the ketomethylene tripeptide fmoc-Nα-Asp(tBu)-(R,S Tyr(tBu)Ψ(CO-CH2)Gly-OH
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A quantitative protease assay based on the formation of a copper-oligopeptide complex is developed. In this assay, when a tripeptide GGH fragment is cleaved from an oligopeptide chain by serine proteases, the tripeptide quickly forms a pink GGH/Cu(2+) complex whose concentration can be determined quantitatively by using UV-Vis spectroscopy. Therefore, activities of serine proteases can be determined from the formation rate of the GGH/Cu(2+) complex. This principle can be used to detect the presence of serine protease in a real-time manner, or measure proteolytic activities of serine protease cleaving different oligopeptide substrates. For example, by using this assay, we demonstrate that trypsin, a model serine protease, is able to cleave two oligopeptides GGGGKGGH () and GGGGRGGH (). However, the specificity constant (kcat/Km) for is higher than that of (6.4 × 10(3) mM(-1) min(-1)vs. 1.3 × 10(3) mM(-1) min(-1)). This result shows that trypsin is more specific toward arginine (R) than lysine (K) in the oligopeptide sequence.
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Proton-dependent oligopeptide transporters (POTs) are important for the uptake of di-/tripeptides in many organisms and for drug transport in humans. The binding mode of dipeptides has been well described. However, it is still debated how tripeptides are recognized. Here, we show that tripeptides of the sequence Phe-Ala-Xxx bind with similar affinities as dipeptides to the POT transporter from Streptococcus thermophilus (PepTSt ). We furthermore determined a 2.3-Å structure of PepTSt in complex with Phe-Ala-Gln. The phenylalanine and alanine residues of the peptide adopt the same positions as previously observed for the Phe-Ala dipeptide, while the glutamine side chain extends into a hitherto uncharacterized pocket. This pocket is adaptable in size and can likely accommodate a wide variety of peptide side chains.
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Abstract The synthesis and characterization of a series of oligopeptides (from the tripeptide to the octadecapeptide) with the repeating sequence L ‐norvalyl‐glycyl‐ L ‐proline and a polytripeptide with this sequence are reported. The oligomers were synthesized step by step using the mixed anhydride method. All the products were chemically and optically pure. The polymer was prepared by the active ester method, using the p ‐nitrophenyl ester as the polymerizable tripeptide derivative. Good yield of relatively high average molecular‐weight polymer was obtained. In the accompanying paper conformational investigations, both in solution and in the solid state, on the oligomers and the polymer are described.
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Electrochemical gradient
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Abstract In this paper, we describe the predominant conformational forms adopted by tripeptides and higher oligopeptides in aqueous solution. About 50 tripeptides and almost 20 higher oligopeptides (4–6 residues) were subjected to conformational analysis using SYBYL Random Search. As with dipeptides (Grail BM, Payne JW. J. Peptide Sci. 2000; 6: 186–199), both tripeptides and higher oligopeptides were found to occupy relatively few combinations of psi–phi space that were distinct from those associated with predominant protein secondary structures (e.g. helices and β‐sheets). Again, the preferred psi (ψ) values for the first residue ( i −1) were in sectors encompassed by the ranges from +150° to ±180°, +60° to +90° and −60° to −90°, which were combined with preferred phi (ϕ) values for the second residue ( i ) in sectors with ranges from −150° to ±180°, −60° to −90° and +30° to +60°. It was notable that tripeptides and, to a greater extent, higher oligopeptides adopted an initial psi (ψ) (Tor2) from +150° to ±180°. For tripeptides, their N – C distances (distance between N ‐terminal nitrogen and C ‐terminal carbon atoms) distribute about 6.5 Å to give shorter, ‘folded’ conformers that are similar in length to dipeptides, and longer, ‘extended’ conformers that are distinct. Furthermore, for higher oligopeptides, their N – C distances did not increment in relation to their increasing number of residues and short, ‘folded’ conformers were still present. These findings have a bearing upon the recognition of these molecules as substrates for widely distributed peptidases and peptide transporters. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.
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Electrochemical gradient
Isothermal Titration Calorimetry
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Lactococcus lactis ML3 possesses two different peptide transport systems of which the substrate size restriction and specificity have been determined. The first system is the earlier-described proton motive force-dependent di-tripeptide carrier (E. J. Smid, A. J. M. Driessen, and W. N. Konings, J. Bacteriol. 171:292-298, 1989). The second system is a metabolic energy-dependent oligopeptide transport system which transports peptides of four to at least six amino acid residues. The involvement of a specific oligopeptide transport system in the utilization of tetra-alanine and penta-alanine was established in a mutant of L. lactis MG1363 that was selected on the basis of resistance to toxic analogs of alanine and alanine-containing di- and tripeptides. This mutant is unable to transport alanine, dialanine, and trialanine but still shows uptake of tetra-alanine and penta-alanine. The oligopeptide transport system has a lower activity than the di-tripeptide transport system. Uptake of oligopeptides occurs in the absence of a proton motive force and is specifically inhibited by vanadate. The oligopeptide transport system is most likely driven by ATP or a related energy-rich, phosphorylated intermediate.
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Amide
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