2 Matching Annotations
  1. Jul 2018
    1. On 2017 Aug 04, Luis Mauricio T. R. Lima commented:

      This is an interesting article showing the pramlintide and zinc interaction, and the role of His18 in zinc interaction such as previously reported for human amylin. https://www.ncbi.nlm.nih.gov/pubmed/20536124 https://doi.org/10.1021/ja1007867

      We have also recently reported (2016) the amyloid aggregation of pramlintide, spontaneously and without zinc. https://www.ncbi.nlm.nih.gov/pubmed/27665170 https://doi.org/10.1016/j.bpc.2016.09.007

      Murine amylin, another "stable" (compared to human) amylin analogue, also behaves as amyloid in solution. https://www.ncbi.nlm.nih.gov/pubmed/23974296 https://doi.org/10.1016/j.bpc.2013.07.013

      Murine amylin can also interact with zinc, and this peptide has no His18, and interaction is mediated by several other contacts, and can result in modulation of the amyloid aggregation process. https://www.ncbi.nlm.nih.gov/pubmed/27693831 http://dx.doi.org/10.1016/j.bpc.2016.09.008

      Collectively, these data suggest an universal amyloid behavior of amylin analogues and interaction with zinc, regardless of the presence of proline or His18.


      This comment, imported by Hypothesis from PubMed Commons, is licensed under CC BY.

  2. Feb 2018
    1. On 2017 Aug 04, Luis Mauricio T. R. Lima commented:

      This is an interesting article showing the pramlintide and zinc interaction, and the role of His18 in zinc interaction such as previously reported for human amylin. https://www.ncbi.nlm.nih.gov/pubmed/20536124 https://doi.org/10.1021/ja1007867

      We have also recently reported (2016) the amyloid aggregation of pramlintide, spontaneously and without zinc. https://www.ncbi.nlm.nih.gov/pubmed/27665170 https://doi.org/10.1016/j.bpc.2016.09.007

      Murine amylin, another "stable" (compared to human) amylin analogue, also behaves as amyloid in solution. https://www.ncbi.nlm.nih.gov/pubmed/23974296 https://doi.org/10.1016/j.bpc.2013.07.013

      Murine amylin can also interact with zinc, and this peptide has no His18, and interaction is mediated by several other contacts, and can result in modulation of the amyloid aggregation process. https://www.ncbi.nlm.nih.gov/pubmed/27693831 http://dx.doi.org/10.1016/j.bpc.2016.09.008

      Collectively, these data suggest an universal amyloid behavior of amylin analogues and interaction with zinc, regardless of the presence of proline or His18.


      This comment, imported by Hypothesis from PubMed Commons, is licensed under CC BY.