2002 Fiscal Year Final Research Report Summary
Mechanisms accelerating tachykinin's biological activities
| Project/Area Number |
13671959
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Functional basic dentistry
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| Research Institution | Fukuoka Dental College |
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Principal Investigator |
ABE Kimio Fukuoka Dental College, Functional Bioscience, Prof., 歯学部, 教授 (70076016)
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| Project Period (FY) |
2001 – 2002
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| Keywords | Tachykinin / Active site / Sialogogue / Salivary Gland / Oligopeptide / Rat / Aminosequence / Synthetic peptide |
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| Research Abstract |
The biological activities of natural and synthetic tachykinins are elaborately controlled in the amino acid sequence. Especially methionylamide (M-NH2), a terminal amino acid, and phenylalanine (F) including in a C-terminal pentapeptide are essential to keep tachykinin's activities and to work as an address domain for the NK receptors. However, there are many other regulatory mechanisms in not only C-terminals but N-terminals. When a C-terminal heptapeptide has strong activity, the N-terminals work inhibitedly and vice visa. In addition, the intensity of biological activities are drastically dependent on the combination mode of three amino acids in positions 5, 6 and 8 present in amino acid sequence. The D-type amino acids are also replaceable with L-type ones. The nonapeptide (QKQQFYGLM-NH2) with the strongest activities for salivation has newly been determined, but its dimmer does not show any effectiveness for salivation. We have carried out using many synthetic tachykinins to find out the active site for salivation. But, it is very complicated to elucidate how to control the active site. Unfortunately the nonapeptide was too short to determine the secondary or tertiary structure with a high technology machine.
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Research Products
(11 results)
