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    Prospects in the use of aptamers for characterizing the structure and stability of bioactive proteins and peptides in food

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    Authors
    Agyei, D.
    Acquah, C.
    Tan, K.
    Hii, H.
    Rajendran, S.
    Udenigwe, C.
    Danquah, Michael
    Date
    2018
    Type
    Journal Article
    
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    Citation
    Agyei, D. and Acquah, C. and Tan, K. and Hii, H. and Rajendran, S. and Udenigwe, C. and Danquah, M. 2018. Prospects in the use of aptamers for characterizing the structure and stability of bioactive proteins and peptides in food. Analytical and Bioanalytical Chemistry. 410 (2): pp. 297-306.
    Source Title
    Analytical and Bioanalytical Chemistry
    DOI
    10.1007/s00216-017-0599-9
    ISSN
    1618-2642
    School
    Curtin Malaysia
    URI
    http://hdl.handle.net/20.500.11937/67423
    Collection
    • Curtin Research Publications
    Abstract

    Food-derived bioactive proteins and peptides have gained acceptance among researchers, food manufacturers and consumers as health-enhancing functional food components that also serve as natural alternatives for disease prevention and/or management. Bioactivity in food proteins and peptides is determined by their conformations and binding characteristics, which in turn depend on their primary and secondary structures. To maintain their bioactivities, the molecular integrity of bioactive peptides must remain intact, and this warrants the study of peptide form and structure, ideally with robust, highly specific and sensitive techniques. Short single-stranded nucleic acids (i.e. aptamers) are known to have high affinity for cognate targets such as proteins and peptides. Aptamers can be produced cost-effectively and chemically derivatized to increase their stability and shelf life. Their improved binding characteristics and minimal modification of the target molecular signature suggests their suitability for real-time detection of conformational changes in both proteins and peptides. This review discusses the developmental progress of systematic evolution of ligands by exponential enrichment (SELEX), an iterative technology for generating cost-effective aptamers with low dissociation constants (K d ) for monitoring the form and structure of bioactive proteins and peptides. The review also presents case studies of this technique in monitoring the structural stability of bioactive peptide formulations to encourage applications in functional foods. The challenges and potential of aptamers in this research field are also discussed.

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