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1. Full Text Synthetic cationic amphiphilic α -helical peptides as antimicrobial agents
by Wiradharma, Nikken and Khoe, Ulung and Hauser, Charlotte A.E and Seow, See Voon and Zhang, Shuguang and Yang, Yi-Yan
Biomaterials, ISSN 0142-9612, 2010, Volume 32, Issue 8, pp. 2204 - 2212
Advanced Basic Science | Dentistry | Hemolysis | α-Helix | Membrane lysis | Antimicrobial peptides (AMP) | Minimum inhibitory concentration (MIC) | Engineering | Materials Science | Technology | Engineering, Biomedical | Materials Science, Biomaterials | Science & Technology | Hemolysis - drug effects | Amino Acid Sequence | Cations - chemistry | Peptides - chemistry | Protein Structure, Secondary | Antimicrobial Cationic Peptides - chemistry | Anti-Infective Agents - pharmacology | Humans | Antimicrobial Cationic Peptides - pharmacology | Peptides - genetics | Molecular Sequence Data | Rats | Peptides - pharmacology | Microbial Sensitivity Tests | Animals | Candida albicans - drug effects | Cations - pharmacology | Anti-Infective Agents - chemistry | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Antimicrobial Cationic Peptides - genetics | Circular Dichroism | Bacillus subtilis - drug effects | Index Medicus
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2. Full Text Production of the angiotensin I converting enzyme inhibitory peptides and isolation of four novel peptides from jellyfish (Rhopilema esculentum) protein hydrolysate
by Liu, Xin and Zhang, Miansong and Shi, Yaping and Qiao, Ruojin and Tang, Wei and Sun, Zhenliang
Journal of the science of food and agriculture, ISSN 0022-5142, 07/2016, Volume 96, Issue 9, pp. 3240 - 3248
ACE inhibitory peptide | response surface methodology | jellyfish | protein hydrolysate | Jellyfish | Protein hydrolysate | Response surface methodology | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Food Science & Technology | Agriculture, Multidisciplinary | Agriculture | Science & Technology | Amino Acid Sequence | Protein Hydrolysates - metabolism | Temperature | Protein Hydrolysates - chemistry | Peptides - chemistry | Angiotensin-Converting Enzyme Inhibitors - metabolism | Protein Hydrolysates - antagonists & inhibitors | Enzyme Assays | Scyphozoa - chemistry | Chromatography, High Pressure Liquid | Angiotensin-Converting Enzyme Inhibitors - isolation & purification | Protein Hydrolysates - isolation & purification | Peptides - isolation & purification | Animals | Peptides - metabolism | Inhibitory Concentration 50 | Enzyme Activation | Hydrogen-Ion Concentration | Proteins | Hydrolysis | Protein hydrolysates | Angiotensin | Angiotensin converting enzyme | Glycine | Glutamine | Seafood | Food science | Peptides | ACE inhibitors | Functional foods & nutraceuticals | Index Medicus | Enzymes | Human body | Converting | Foods | Hydrolysates
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3. Full Text Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats
by Balti, Rafik and Bougatef, Ali and Sila, Assaâd and Guillochon, Didier and Dhulster, Pascal and Nedjar-Arroume, Naima
Food chemistry, ISSN 0308-8146, 03/2015, Volume 170, pp. 519 - 525
Cuttlefish muscle protein | ACE inhibitory peptide | Enzymatic hydrolysate | Purification and identification | Antihypertensive effect | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Nutrition & Dietetics | Food Science & Technology | Science & Technology | Rats, Inbred SHR | Amino Acid Sequence | Antihypertensive Agents - pharmacology | Angiotensin-Converting Enzyme Inhibitors - analysis | Molecular Weight | Protein Hydrolysates - chemistry | Rats | Male | Angiotensin-Converting Enzyme Inhibitors - isolation & purification | Hypertension - pathology | Peptides - pharmacology | Antihypertensive Agents - chemistry | Decapodiformes - metabolism | Peptides - isolation & purification | Animals | Spectrometry, Mass, Electrospray Ionization | Muscles - enzymology | Antihypertensive Agents - isolation & purification | Muscles - chemistry | Angiotensin-Converting Enzyme Inhibitors - pharmacology | Blood Pressure - drug effects | Protein Stability | Chromatography, Gel | Peptides - analysis | Hypertension | Enzyme inhibitors | Protein hydrolysates | Angiotensin | Index Medicus
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4. Full Text Preparation of bioactive peptides with antidiabetic, antihypertensive, and antioxidant activities and identification of α‐glucosidase inhibitory peptides from soy protein
by Wang, Rongchun and Zhao, Hongxing and Pan, Xiaoxi and Orfila, Caroline and Lu, Weihong and Ma, Ying
Food science & nutrition, ISSN 2048-7177, 05/2019, Volume 7, Issue 5, pp. 1848 - 1856
peptide | ACE inhibitory activity | α‐glucosidase inhibitory activity | antioxidant activity | antidiabetic activity | soy protein | Life Sciences & Biomedicine | Food Science & Technology | Science & Technology | Soybeans | Alkaline proteinase | CD26 antigen | Peptides | Proteinase | Amino acids | Cardiovascular disease | Small intestine | Molecular weight | Proteins | Antioxidants | Hyperglycemia | Nutraceuticals | Carbohydrates | Enzymes | Peptidase | Nucleotide sequence | Digestive system | Diabetes mellitus | Papain | Glucosidase | Gastrointestinal tract | Digestion | Insulin | Hydrolysates | Trypsin | Anion exchanging | Angiotensin | Diabetes
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5. Full Text Short Photoswitchable Antibacterial Peptides
by Yeoh, Yuan Qi and Horsley, John R and Yu, Jingxian and Polyak, Steven W and Jovcevski, Blagojce and Abell, Andrew D
ChemMedChem, ISSN 1860-7179, 08/2020, Volume 15, Issue 16, pp. 1505 - 1508
hydrophobicity | amphiphilicity | azobenzene photoswitch | Staphylococcus aureus | antibacterial peptides | Antibiotics | Peptides | Minimum inhibitory concentration | Azo compounds | Antibacterial activity | Chains | Lipids | Hydrophobicity | Secondary structure | Protein structure | Index Medicus
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6. Full Text Antihypertensive peptides from animal products, marine organisms, and plants
by Lee, Seung Yun and Hur, Sun Jin
Food chemistry, ISSN 0308-8146, 08/2017, Volume 228, pp. 506 - 517
Animal products | Marine organisms | Peptide sequences | Plants | ACE-inhibitory peptide | Enzymatic hydrolysis | Physical Sciences | Chemistry | Life Sciences & Biomedicine | Chemistry, Applied | Nutrition & Dietetics | Food Science & Technology | Science & Technology | Aquatic Organisms - cytology | Amino Acid Sequence | Antihypertensive Agents - chemistry | Animals | Peptides - chemistry | Aquatic Organisms - metabolism | Angiotensin-Converting Enzyme Inhibitors - chemistry | Hydrolysis | Chymotrypsin | Trypsin | Biological products | Peptides | Proline | Angiotensin | Index Medicus
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7. Full Text Glucose-Dependent Insulinotropic Peptide Stimulates Glucagon-Like Peptide 1 Production by Pancreatic Islets via Interleukin 6, Produced by α Cells
by Timper, Katharina and Dalmas, Elise and Dror, Erez and Rütti, Sabine and Thienel, Constanze and Sauter, Nadine S and Bouzakri, Karim and Bédat, Benoit and Pattou, Francois and Kerr-Conte, Julie and Böni-Schnetzler, Marianne and Donath, Marc Y
Gastroenterology (New York, N.Y. 1943), ISSN 0016-5085, 2016, Volume 151, Issue 1, pp. 165 - 179
Gastroenterology and Hepatology | Immune Regulation | Incretin | Hormones | Mouse Model | Gastroenterology & Hepatology | Life Sciences & Biomedicine | Science & Technology | Gastric Inhibitory Polypeptide - metabolism | Humans | Mice, Inbred C57BL | Glucagon-Like Peptide 1 - biosynthesis | Insulin - metabolism | Insulin-Secreting Cells - metabolism | Animals | Diabetes Mellitus, Experimental - etiology | Glucagon-Secreting Cells - metabolism | Mice | Blood Glucose - metabolism | Diabetes Mellitus, Experimental - metabolism | Insulin Secretion | Interleukin-6 - metabolism | Index Medicus | Abridged Index Medicus
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8. Full Text Stability to gastrointestinal enzymes and structure–activity relationship of β-casein-peptides with antihypertensive properties
by Quirós, Ana and Contreras, María del Mar and Ramos, Mercedes and Amigo, Lourdes and Recio, Isidra
Peptides (New York, N.Y. : 1980), ISSN 0196-9781, 2009, Volume 30, Issue 10, pp. 1848 - 1853
Antihypertensive activity | Competitive inhibitors | ACE-inhibitory peptides | Simulated gastrointestinal digestion | Fermented milk | Pharmacology & Pharmacy | Biochemistry & Molecular Biology | Endocrinology & Metabolism | Life Sciences & Biomedicine | Science & Technology | Fundamental and applied biological sciences. Psychology | Vertebrates: endocrinology | Biological and medical sciences | Amino Acid Sequence | Milk - chemistry | Peptides - chemistry | Caseins - genetics | Caseins - metabolism | Molecular Sequence Data | Structure-Activity Relationship | Antihypertensive Agents - metabolism | Fermentation | Digestion - physiology | Antihypertensive Agents - chemistry | Animals | Peptides - metabolism | Caseins - chemistry | Protein Conformation | Gastrointestinal Tract - enzymology | Index Medicus
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9. Full Text Antihypertensive peptides: Production, bioavailability and incorporation into foods
by Hernández-Ledesma, Blanca and del Mar Contreras, María and Recio, Isidra
Advances in colloid and interface science, ISSN 0001-8686, 2011, Volume 165, Issue 1, pp. 23 - 35
Stability | Bioavailability | Antihypertensive peptides | Fermentation | Enzymatic hydrolysis | Angiotensin-converting enzyme inhibitory activity | Amino Acid Sequence | Antihypertensive Agents - pharmacology | Protein Biosynthesis | Peptides - chemistry | Humans | Peptides - pharmacokinetics | Biological Availability | Structure-Activity Relationship | Antihypertensive Agents - metabolism | Antihypertensive Agents - pharmacokinetics | Peptides - pharmacology | Antihypertensive Agents - chemistry | Animals | Peptides - metabolism | Food | Hydrolysis | Peptides | Physiological aspects | Index Medicus | Receiving | Focusing | Bacteria | Foods
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