Weihong Lu
Harbin Institute of Technology
34 Papers
3 Citations
Weihong Lu is an academic researcher from Harbin Institute of Technology. The author has contributed to research in topics: Medicine & Biology. The author has an hindex of 13, co-authored 16 publications.
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Papers
Advancement and prospects of bioinformatics analysis for studying bioactive peptides from food-derived protein: Sequence, structure, and functions
TL;DR: An overview of research progress in the bioinformatics methods used for identifying, characterizing, elaborating bioactive mechanisms of, and producing food-derived bioactive peptides is provided to present an effective workflow.
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Characterization of natural hydroxyapatite originated from fish bone and its biocompatibility with osteoblasts.
TL;DR: The nHAP originated from rainbow trout and salmon bones have a great potential for application as implant material substitute in bone tissue engineering and the natural waste fish bone product can be used for hydroxyapatite synthesis as a part of bio-waste management.
178
Identification of a novel ACE-inhibitory peptide from casein and evaluation of the inhibitory mechanisms.
TL;DR: A novel angiotensin I-converting enzyme (ACE)-inhibitory (ACEI) peptide, NMAINPSKENLCSTFCK, derived from the αs2-casein fragment residues 25-41, was screened and identified by UPLC-ESI-Q-TOF-MS/MS from tryptic casein hydrolysate and showed that this peptide acted as a mixed-type inhibitor against ACE.
177
Preparation of bioactive peptides with antidiabetic, antihypertensive, and antioxidant activities and identification of α-glucosidase inhibitory peptides from soy protein.
TL;DR: In this paper, the peptides of soy protein obtained by enzymatic digestion with proteases were analyzed for their antidiabetic, antihypertensive, and antioxidant activities.
168
Sequence analysis and molecular docking of antithrombotic peptides from casein hydrolysate by trypsin digestion
TL;DR: Thrombin inhibitory peptides from casein were screened by bioinformatics based on sequences predicted from in silico enzymatic digestion with trypsin, and identified by UPLC-Q-TOF-MS/MS with Mascot analysis.
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