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Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins
Abstract
Two antimicrobial peptides (Ac-AMP1 and Ac-AMP2) were isolated from seeds of amaranth (Amaranthus caudatus), and their physicochemical and biological properties were characterized. On the basis of fast atom bombardment mass spectroscopy, Ac-AMP1 and Ac-AMP2 have monoisotopic molecular masses of 3025 and 3181, respectively. Both proteins have pI values above 10. The amino acid sequence of Ac-AMP1 (29 residues) is identical to that of Ac-AMP2 (30 residues), except that the latter has 1 additional residue at the carboxyl terminus. The sequences are highly homologous to the cysteine/glycine-rich domain occurring in many chitin-binding proteins. Both Ac-AMP1 and Ac-AMP2 bind to chitin in a reversible way. Ac-AMP1 and Ac-AMP2 inhibit the growth of different plant pathogenic fungi at much lower doses than other known antifungal chitin-binding proteins. In addition, they show some activity on Gram-positive bacteria. The antimicrobial effect of Ac-AMP1 and Ac-AMP2 is strongly antagonized by cations.
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Citations
Cited by
Lectins as Plant Defense Proteins
Peumans, W. J., & Van Damme, E. (1995) · Plant Physiology · doi:10.1104/pp.109.2.347 · Cited by 1,160
Antimicrobial Peptides from Plants
Broekaert, W. F., Cammue, B. P. A., De Bolle, M. F. C., Thevissen, K., De Samblanx, G. W., Osborn, R. W., & Nielson, K. (1997) · Critical Reviews in Plant Sciences · doi:10.1080/07352689709701952 · Cited by 678
Self-citationBachère, E., Gueguen, Y., Gonzalez, M., De Lorgeril, J., Garnier, J., & Romestand, B. (2004) · Immunological Reviews · doi:10.1111/j.0105-2896.2004.00115.x · Cited by 507
Lehrer, R. I. (2004) · Nature Reviews Microbiology · doi:10.1038/nrmicro976 · Cited by 448
Osborn, R. W., De Samblanx, G. W., Thevissen, K., Goderis, I., Torrekens, S., Van Leuven, F., Attenborough, S., Rees, S. B., & Broekaert, W. F. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)00666-w · Cited by 391
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Metadata
- Authors
- Broekaert, W. F., Marien, W., Terras, F. R. G., De Bolle, M. F. C., Proost, P., Van Damme, J., Dillen, L., Claeys, M., & Rees, S. B.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1992-05-15
- Volume
- 31
- Issue
- 17
- Pages
- 4308-4314
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2048900330
- Cited by
- 345
- References
- 0
- FWCI
- 9.14
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. https://app.cochat.ai/papers/10.1021/bi00132a023
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- Broekaert, W. F., Marien, W., Terras, F. R. G., De Bolle, M. F. C., Proost, P., Van Damme, J., Dillen, L., Claeys, M., & Rees, S. B. (1992). Antimicrobial peptides from Amaranthus caudatus seeds with sequence homology to the cysteine/glycine-rich domain of chitin-binding proteins. Biochemistry. https://doi.org/10.1021/bi00132a023
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