Yiotakis A, Lecoq A, Nicolaou A, Labadie J, Dive V
Department of Organic Chemistry, University of Athens, Greece.
Biochem J. 1994 Oct 1;303 ( Pt 1)(Pt 1):323-7. doi: 10.1042/bj3030323.
Pseudo-substrate analogues of collagenase from Corynebacterium rathayii, in which the scissile peptide bond is replaced by a phosphinic moiety, were synthesized and evaluated as inhibitors of this enzyme. The phosphinic tetrapeptide, Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1), was found to be a potent inhibitor of collagenase with a Ki value of 8 nM. Increasing the length of the phosphinic-containing inhibitors from tetra- to hepta-peptide size further improves the potency of these compounds. The heptapeptide analogue, Z-Phe-Gly-Pro-Phe-psi(PO2CH2)-Gly-Pro-Nle-OMe, with a Ki value of 0.6 nM, is the most potent inhibitor reported to date for bacterial collagenases. A comparison between the phosphinic analogue Z-Phe-psi(PO2CH2)-Gly-Pro-Nle (1) and the phosphonamide peptide Z-Phe-psi(PO2NH)-Gly-Pro-Nle (2) shows that for bacterial collagenase the replacement of a CH2 by an NH group results only in a modest increase in affinity from Ki = 8 nM for compound 1 to Ki = 6 nM for compound 2. Most of the phosphorus-containing inhibitors of this series are slow- or slow-tight-binding inhibitors with second-order rate constants for association and dissociation varying respectively for the kon values from 1 x 10(3) to 26 x 10(3) M-1.s-1 and for the koff values from 3 x 10(-4) to 2 x 10(-5) s-1. Interestingly, the lower affinity of the molecule containing a D residue in the P1 position of the inhibitor, compared with the molecule with an L residue in this position, is mainly the consequence of a lower rate constant for association of these D stereoisomers with the enzyme. This study demonstrates that phosphinic peptide analogues are potent inhibitors of a bacterial collagenase. The development of new phosphinic peptides should lead to the discovery of potent inhibitors of other zinc metalloproteases. Details of how the analogues were synthesized are given in Supplementary Publication SUP 50176 (14 pages), which has been deposited with the British Library Document Supply Centre, Boston Spa, Wetherby, W. Yorkshire LS23 7BQ, from whom copies can be obtained on the terms indicated in Biochem. J. (1994) 297, 9.
合成了来自拉氏棒杆菌胶原酶的伪底物类似物,其中可裂解肽键被次膦酸部分取代,并对其作为该酶的抑制剂进行了评估。发现次膦酸四肽Z-Phe-ψ(PO₂CH₂)-Gly-Pro-Nle(1)是胶原酶的有效抑制剂,其Ki值为8 nM。将含次膦酸的抑制剂长度从四肽增加到七肽大小可进一步提高这些化合物的效力。七肽类似物Z-Phe-Gly-Pro-Phe-ψ(PO₂CH₂)-Gly-Pro-Nle-OMe的Ki值为0.6 nM,是迄今为止报道的对细菌胶原酶最有效的抑制剂。次膦酸类似物Z-Phe-ψ(PO₂CH₂)-Gly-Pro-Nle(1)与磷酰胺肽Z-Phe-ψ(PO₂NH)-Gly-Pro-Nle(2)的比较表明,对于细菌胶原酶,用NH基团取代CH₂仅导致亲和力适度增加,从化合物1的Ki = 8 nM增加到化合物2的Ki = 6 nM。该系列中大多数含磷抑制剂是慢结合或慢紧密结合抑制剂,其缔合和解离的二级速率常数分别为kon值从1×10³到26×10³ M⁻¹·s⁻¹,koff值从3×10⁻⁴到2×10⁻⁵ s⁻¹。有趣的是,与在该位置含有L残基的分子相比,抑制剂P1位置含有D残基的分子亲和力较低,主要是这些D立体异构体与酶缔合的速率常数较低的结果。这项研究表明次膦酸肽类似物是细菌胶原酶的有效抑制剂。新型次膦酸肽的开发应会导致发现其他锌金属蛋白酶的有效抑制剂。类似物的合成细节见补充出版物SUP 50176(14页),该出版物已存放在英国图书馆文献供应中心,地址为西约克郡韦瑟比市波士顿温泉LS23 7BQ,可按《生物化学杂志》(1994年)297卷9期所示条件从该处获取复印件。