Conomarphins cause paralysis in mollusk: Critical and tunable structural elements for bioactivity
| Autor: | Dessa Camille R Batoctoy, Lilibeth A. Salvador-Reyes, Arturo O. Lluisma, Charmaine B Mendoza, Eizadora T. Yu, Dan Jethro M Masacupan |
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| Rok vydání: | 2019 |
| Předmět: |
animal structures
Venom 010402 general chemistry 01 natural sciences Biochemistry Structure-Activity Relationship Structural Biology Drug Discovery Animals Amino Acid Sequence Conidae Molecular Biology Pharmacology chemistry.chemical_classification biology 010405 organic chemistry Chemistry Organic Chemistry Conus Snail Biological activity General Medicine Siphon (mollusc) biology.organism_classification Pomacea 0104 chemical sciences Amino acid Mollusca Posttranslational modification Molecular Medicine Conus eburneus Conotoxins |
| Zdroj: | Journal of Peptide Science. 25 |
| ISSN: | 1099-1387 1075-2617 |
| DOI: | 10.1002/psc.3179 |
| Popis: | Two conomarphins were purified as the major component of the venom of Conus eburneus. Conomarphins Eb1 and Eb2 showed biological activity in the mollusk Pomacea padulosa, causing sluggishness and retraction of siphon, foot, and cephalic tentacles. To further probe the effects of conserved amino acids and posttranslational modifications in conomarphins, we prepared four synthetic analogues: conomarphin Eb1 Hyp10Pro, Hyp10Ala, d-Phe13Ala, and l-Phe13 variants. Structure-activity relationship analysis indicated that d-Phe13 is critical to the biological activity of conomarphins. In contrast, amino acid changes at position 10 and removal of posttranslational modification in Hyp10Pro can be tolerated. The high expression level and observed mollusk activity of conomarphins may suggest their potential role as defensive arsenal of Conoidean snails against other predatory gastropods. |
| Databáze: | OpenAIRE |
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