Amphiphilic growth hormone releasing factor (GRF) analogs: peptide design and biological activity in vivo |
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| Authors: | J S Tou L A Kaempfe B D Vineyard F C Buonomo M A Della-Fera C A Baile |
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| Institution: | 1. College of Animal Science, Inner Mongolia Agricultural University, Hohhot 010018, China;2. Youmute Farming Co., Ltd., Hohhot 011517, China;1. Nucleo di Ricerca sulla Desertificazione (NRD), Università di Sassari, Viale Italia 39, 07100 Sassari, Italy;2. Dipartimento di Scienze della Natura e del Territorio, Università di Sassari, Via Piandanna 4, 07100 Sassari, Italy;1. Department of Agronomy and Plant Breeding, Faculty of Agriculture, Ferdowsi University of Mashhad, Mashhad, Iran;2. Agricultural Research, Education and Extension Organization (AREEO), Sanandaj, Iran;1. The Robert H. Smith Institute for Plant Sciences and Genetics in Agriculture, Faculty of Agricultural, Food and Environmental Sciences, Hebrew University of Jerusalem, Rehovot 76100, Israel;2. Department of Natural Resources, ARO − The Volcani Center, P.O. Box 6, Bet-Dagan 50250, Israel;3. MIGAL − Galilee Technological Center, Qiryat Shemona, P.O. Box 90000, Rosh Pina 12100, Israel;4. Beef Cattle Section, Newe-Ya''ar Research Center, Department of Natural Resources, Agricultural Research Organization, P.O. Box 1021, Ramat Yishay 30095, Israel |
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| Abstract: | The first twenty-nine amino acids of human Growth Hormone Releasing Factor (hGRF) possess a distinct amphiphilic character. This is seen as twisted hydrophobic and hydrophilic bands in the helical net projection. Four amidated analogs were designed by optimizing amphiphilic and helical potentials of the native sequence. These designed analogs, with up to eight-amino acid changes, were tested in sheep via intravenous injection. The growth hormone-stimulating activities of the analogs were significantly higher when compared to bovine Growth Hormone Releasing Factor (bGRF44-NH2). This suggests that the amphiphilic conformation of GRF(1-29) is important to the receptor. |
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