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Hydrocarbon stapling enables improvement of antimicrobial activity and proteolytic stability of host‐defense peptide ocellatin‐3N
Supporting Information As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
All‐hydrocarbon stapling enables improvement of antimicrobial activity and proteolytic stability of peptide Figainin 2
CONFLICT OF INTEREST STATEMENT The authors declare no conflict of interest. Supporting Information Filename Description psc3566-supp-0001-Supporting Information.docxWord 2007 document , 564.2 KB Table S1. Electrospray MS data for peptides (positive mode) Figure S1. Preparation of peptide 1. Peptide 1 was purified by HPLC (purification conditions: 10% - 75% CH3CN (0.1% TFA) in H2O (0.1% TFA) over 55 min on a Welch C18 column). peptide 1 was obtained with an isolated yield of 11.83%.
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