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However, certain characteristics of pramlintide pharmacokinetics and formulation leave considerable room for further development of amylin\u2010mimetic compounds. Given that amylin\u2010mimetic drug design and development is an active area of research, surprisingly little is known about the structure\/function relationships of amylin. This is largely due to the unfavourable aggregative and solubility properties of the native peptide sequence, which are further complicated by the composition of amylin receptors. These are complexes of the calcitonin receptor with receptor activity\u2010modifying proteins. This review explores what is known of the structure\u2013function relationships of amylin and provides insights that can be drawn from the closely related peptide, CGRP. We also describe how this information is aiding the development of more potent and stable amylin mimetics, including peptide hybrids.<\/jats:p>","DOI":"10.1111\/bph.13496","type":"journal-article","created":{"date-parts":[[2016,4,10]],"date-time":"2016-04-10T18:31:31Z","timestamp":1460313091000},"page":"1883-1898","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":110,"title":["Amylin structure\u2013function relationships and receptor pharmacology: implications for amylin mimetic drug development"],"prefix":"10.1111","volume":"173","author":[{"given":"Rebekah L","family":"Bower","sequence":"first","affiliation":[{"name":"School of Biological Sciences and Maurice Wilkins Centre for Molecular Biodiscovery University of Auckland Auckland New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9558-5122","authenticated-orcid":false,"given":"Debbie L","family":"Hay","sequence":"additional","affiliation":[{"name":"School of Biological Sciences and Maurice Wilkins Centre for Molecular Biodiscovery University of Auckland Auckland New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2016,5,18]]},"reference":[{"key":"e_1_2_13_2_1","doi-asserted-by":"publisher","DOI":"10.1155\/2016\/2798269"},{"key":"e_1_2_13_3_1","doi-asserted-by":"publisher","DOI":"10.1210\/endo.136.12.7588285"},{"key":"e_1_2_13_4_1","doi-asserted-by":"publisher","DOI":"10.1111\/bph.13348"},{"key":"e_1_2_13_5_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1008365322148"},{"key":"e_1_2_13_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/S1056-8719(00)00074-5"},{"key":"e_1_2_13_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.peptides.2005.11.014"},{"key":"e_1_2_13_8_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1476-5381.2011.01717.x"},{"key":"e_1_2_13_9_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1476-5381.2011.01525.x"},{"key":"e_1_2_13_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/jms.3338"},{"key":"e_1_2_13_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2015.04.018"},{"key":"e_1_2_13_12_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1399-3011.1996.tb01098.x"},{"key":"e_1_2_13_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/0014-5793(92)80362-K"},{"key":"e_1_2_13_14_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpj.2013.07.029"},{"key":"e_1_2_13_15_1","doi-asserted-by":"publisher","DOI":"10.1152\/ajpendo.1998.274.5.E827"},{"key":"e_1_2_13_16_1","doi-asserted-by":"crossref","first-page":"718","DOI":"10.1016\/S0022-3565(25)20868-0","article-title":"Structure\u2013activity profile of calcitonin gene\u2010related peptide in peripheral and brain tissues. 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