Yes / There are many human oral antimicrobial peptides responsible for playing important
roles including maintenance, repairing of oral tissues (hard or soft) and defense against oral
microbes. In this review we have highlighted the biochemistry, physiology and proteomics of human
oral histatin peptides, secreted from parotid and submandibular salivary glands in human. The significance
of these peptides includes capability for ionic binding that can kill fungal Candida albicans.
They have histidine rich amino acid sequences (7–12 family members; corresponding to residues
12–24, 13–24, 12–25, 13–25, 5–11, and 5–12, respectively) for Histatin-3. However, Histatin-3 can
be synthesized proteolytically from histatin 5 or 6. Due to their fungicidal response and high
biocompatibility (little or no toxicity), these peptides can be considered as therapeutic agents with
most probable applications for example, artificial saliva for denture wearers and salivary gland
dysfunction conditions. The objectives of current article are to explore the human histatin peptides
for its types, chemical and biological aspects. In addition, the potential for therapeutic bio-dental
applications has been elaborated. / King Saud University
| Identifer | oai:union.ndltd.org:BRADFORD/oai:bradscholars.brad.ac.uk:10454/8907 |
| Date | 04 May 2016 |
| Creators | Khurshid, Z., Najeeb, S., Mali, M., Moin, S.F., Raza, S.Q., Zohaib, S., Sefat, Farshid, Zafar, M.S. |
| Source Sets | Bradford Scholars |
| Language | English |
| Detected Language | English |
| Type | Article, published version paper |
| Rights | © 2016 The Authors. This is an open access article licensed under the Crative Commons CC-BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/) |
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