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【作者】Pignatello, R. and T. M. Pecora 【文题】"Conjugation of thymopentin (TP5) with lipoamino acid residues increases the hydrolytic stability and preserves the biological activity." 【期刊名，年份，卷（期），起止页码】(2007). Pharmazie 62(9): 663-7 因为时间紧急！就麻烦大家了！ [ Last edited by colinxu007 on 2008-2-19 at 14:46 ] |
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万方有http://168.160.184.242/wf/mst.dl ... P=I&MFN=5658285 文献类型： 期刊论文 正 题 名： Conjugation of thymopentin (TP5) with lipoamino acid residues increases the hydrolytic stability and preserves the biological activity. 个人作者姓名： Pignatello,R; Pecora,TM; 作者单位： Dipartimento di Scienze Farmaceutiche, Citta Universitaria, viale A. Doria, 6, 1-95125 Catania, Italy. r.pignatello@unict.it 刊 名： Pharmazie,Die 浏览此刊所有论文 出版年份： 2007 年 卷 期： vol.62 浏览此期所有论文 页 码： P.663-667 总页数： 5 分 类 号： R9 关 键 词： Assault by stabbing; Thymopentin; Parents; Acids; LAA; 胸腺喷丁; 双亲; 酸类; 正文语种： eng 文 摘： Three conjugates of thymopentin (TP5), an oligopeptide derived from the thymic hormone thymopoietin, with lipoamino acid (LAAs) have been obtained by solid-phase peptide synthesis. Both linear and dendrimer structures have been prepared to achieve enhanced lipophilicity. After incubation in foetal calf serum the lipophilic conjugates showed a higher stability to hydrolysis with respect to the parent drug. In a preliminary in vitro biological assay, LAA conjugates showed the ability to retain or improve the growth inhibitory activity of the parent peptide against a human lymphoblastoid cell line. The interaction of the prepared conjugates with 1,2-L-alpha-dimiristoylphosphatidylcholine multilamellar liposomes, chosen as a biological membrane model, was studied. The higher lipophilicity of TP5 conjugates was reflected in a better penetration through phospholipid bilayers, whose thermal behaviour was altered in a concentration-dependent way. Such enhanced affinity of TP5-LAA conjugates for this membrane model could anticipate a better interaction with cell membranes and, ultimately, an improved biological activity of compounds compared with the parent pentapeptide. |
2楼2008-02-19 14:04:28