镶嵌在细胞膜上的蛋白质，参与着非常重要的细胞生理反应，就目前药物研发的对象而言，几乎有近三分之二的药物标的，是位于细胞膜上的蛋白质，而就相关的研究数据显示，位居细胞膜下镶嵌着的膜下蛋白，扮演着同样相同的重要角色，不过却因为缺乏着适当的工具，使得探索膜下蛋白的过程，受到了相当程度的阻碍。
这次宾州大学医学院的科学家，以血液凝结的过程为目标，锁定了称为的 integrinsIIb3、 integrinsV3蛋白质，利用蛋白质序列与结构的数据，透过计算机算法的辅助，设计出可以黏着特定膜下蛋白区域的小分子探针 (probes)，据了解血小板上的 integrins蛋白质，和血液的凝结过程中 扮演着关键的重要角色。
目前就研究数据看来，这一个新的探针工具，可以成功的以插入的方式，找到血小板 (platelets)下的 integrins分子，而就这样的一个标示动作来说，科学家可以说找到了一个有效的工具，可以切入膜下蛋白质的研究窗口。
(资料来源 : Bio.com)
原始出处: http://www.bio.com/newsfeatures/newsfeatures_research.jhtml?cid=27600001
部分英文原文：
Science 30 March 2007:
Vol. 315. no. 5820, pp. 1817 - 1822
DOI: 10.1126/science.1136782
Research Articles
Computational Design of Peptides That Target Transmembrane Helices
Hang Yin,1* Joanna S. Slusky,1* Bryan W. Berger,1 Robin S. Walters,1 Gaston Vilaire,2 Rustem I. Litvinov,3 James D. Lear,1 Gregory A. Caputo,1 Joel S. Bennett,2 William F. DeGrado1,4
A variety of methods exist for the design or selection of antibodies and other proteins that recognize the water-soluble regions of proteins; however, companion methods for targeting transmembrane (TM) regions are not available. Here, we describe a method for the computational design of peptides that target TM helices in a sequence-specific manner. To illustrate the method, peptides were designed that specifically recognize the TM helices of two closely related integrins (IIbß3 and vß3) in micelles, bacterial membranes, and mammalian cells. These data show that sequence-specific recognition of helices in TM proteins can be achieved through optimization of the geometric complementarity of the target-host complex.
1 Department of Biochemistry and Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
2 Hematology-Oncology Division, Department of Medicine, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
3 Department of Cell and Developmental Biology, School of Medicine, University of Pennsylvania, Philadelphia, PA 19104, USA.
4 Department of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
* These authors contributed equally to this work.
To whom correspondence should be addressed. E-mail: wdegrado@mail.med.upenn.edu
