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| BRIEF COMMUNICATION |
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| Year : 2010 | Volume
: 2
| Issue : 1 | Page : 47-49 |
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Bioprospecting keratinous materials
LN Jones1, RD Sinclair2, J Carver2, H Ecroyd2, Y Lui2, LE Bennett3
1 Department of Medicine, University of Melbourne, St Vincent's Hospital, Melbourne 3065, Australia
2 Food Science Australia, 3030, Australia
3 School of Chemistry and Physics, University of Adelaide, Australia 5005, Australia
| Date of Web Publication | 29-Jul-2010 |
Correspondence Address:
L N Jones
University of Melbourne, Department of Medicine, St Vincent's Hospital, PO Box 2900, Fitzroy, Victoria - 3065
Australia
 Source of Support: None, Conflict of Interest: None  | Check |
DOI: 10.4103/0974-7753.66915
 Abstract | | |
The concept of bioprospecting for bioactive peptides from keratin-containing materials such as wool, hair, skin and feathers presents an exciting opportunity for discovery of novel functional food ingredients and nutraceuticals, while value-adding to cheap and plentiful natural sources. The published literature reports multiple examples of proline-rich peptides with productive bio-activity in models of human disease including tumour formation, hypertension control and Alzheimer's disease. Bioactive peptides have been identified from food and other protein sources however the bioactivity of keratin-related proteins and peptides is largely unknown. Considering the high representation of proline-rich peptides among proven bioactive peptides, the proline-rich character of keratinous proteins supports current research. A selection of mammalian (cow epidermis, sheep wool) and avian (chicken feather) keratinous materials were subjected to enzymatic hydrolysis using established processing methods. A bio-assay of determining inhibition of early stage amyloid aggregation involved using a model fibril-forming protein - reduced and carboxymethylated bovine K-casein (RCMk-CN) and quantitation of fibril development with the amyloid-specific fluorophore, Thioflavin T (ThT). The assay was fully validated for analytical repeatability and used together with appropriate positive controls. Peptide library products derived from chicken feather (n=9), sheep wool (n=9) and bovine epidermis (n=9) were screened in the fibril inhibition assay based on K-casein. 3 of 27 products exhibited interesting levels of bio-activity with regard to fibril inhibition. HPLC profiles provide an indication of the complexity of the assemblage of peptides in the three active products. We conclude the bioprospecting research using keratinous materials shows promise for discovery of useful bioactive peptides. Keywords: Bioactive peptides, bioprospecting, keratin
How to cite this article:
Jones L N, Sinclair R D, Carver J, Ecroyd H, Lui Y, Bennett L E. Bioprospecting keratinous materials. Int J Trichol 2010;2:47-9 |
| Introduction | |  |
Proline-rich peptides are an important ingredient of a balanced human diet. The modern Western diet is often lacking in these peptides. While dairy products are a major traditional source of these peptides, other low-cost potential sources for dietary supplementation are desirable.
The concept of "bioprospecting" for bioactive peptides from keratin-containing materials such as wool, hair, skin and feathers presents an exciting opportunity for discovery and value-addition. The published literature (scientific and patent) reports multiple examples of proline-rich peptides with protective bioactivity in models of human disease, including tumor formation, hypertension control and Alzheimer's disease. Bioactive peptides have been identified from food and other protein sources. However, the bioactivity of keratin-related proteins and peptides is largely unknown.
Considering the high representation of proline-rich peptides among proven bioactive peptides [Table 1], the proline-rich character of keratinous proteins supports their focus for biodiscovery research.
| Materials and Methods | | |
A selection of mammalian (cow epidermis, sheep wool) and avian (chicken feather) keratinous materials were subjected to enzymatic hydrolysis using established processing methods for library production.
A bioassay for determining inhibition of early-stage amyloid aggregation involved using a model fibril-forming protein (reduced and carboxymethylated bovine kappa-casein, RCM kappa-CN) and quantification of fibril development with the amyloid-specific fluorophore, Thioflavin T ThT, see [Figure 1]. Progressive aggregation of RCK kappa-CN was routinely monitored over 1,000 min by changes in fluorescence (440 nm excitation, 490 nm emission). The assay was fully validated for analytical repeatability and used together with appropriate positive controls.
| Results and Discussion | | |
Peptide library products derived from chicken feather (n=9), sheep wool (n=9) and bovine epidermis (n=9) were screened in the fibril inhibition assay based on kappa-casein. Twenty-seven products were identified; three exhibited sufficient bioactivity to warrant enrichment and identification of active peptides within this sample set [Figure 2].
Results from the primary screening of keratinous peptide libraries in assays related to hypertension, including ACE inhibition and angiotensin II receptor inhibition, also indicate promising bioactivity. As fibril inhibition requires stoichiometric interaction between peptide and kappa-CN, the bioactivity is likely to be associated with most abundant peptides.
High-performance liquid chromatography was used to provide an indication of the complexity of the assemblage of peptides in the three active products [Figure 3].
| Conclusions | | |
Keratinous containing substances such as feather, wool and skin, often discarded after animal slaughter, can now be considered as important future neutraceuticals.
Furthermore, the model systems currently used allow characterization of the molecular properties of fibril-inhibiting peptides and will allow us to elucidate the mechanism and molecular properties of the keratinous peptides responsible for fibril inhibition. Bioprospecting research using keratinous materials facilitates the discovery of useful bioactives in research and product development.[3]
| References | | |
| 1. | Mizuno S, Nishimura S, Matsuura K, Gotou T, Yamamoto N. Release of short and proline-rich antihypertensive peptides from casein hydrolysate with an Aspergillus oryzae protease. J Dairy Sci 2004;87:3183-8.  [PUBMED] [FULLTEXT] |
| 2. | Inglot AD, Janusz M, Lisowski J. Colostrinine: A proline-rich polypeptide from ovine colostrum is a modest cytokine inducer in human leukocytes. Arch Immunol Ther Exp (Warsz) 1996;44:215-24. [PUBMED] |
| 3. | Zhang J, Wong H, Ramanan S, Cheong D, Leong A, Hooi SC. The proline-rich acidic protein is epigenetically regulated and inhibits growth of cancer cell lines. Cancer Res 2003;63:6658-65. [PUBMED] [FULLTEXT] |
[Figure 1], [Figure 2], [Figure 3]
[Table 1]
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