Collagen Peptide Technical Information
Papers related to Nitta Gelatin
FieldYearSection

Author name, Title, Journal name

Absorption

2009

In vivo

Absorption

2012

ClinicalAbsorption

2021

Clinical

Skin

2012

Clinical

Skin

2014

In vivo

Skin

2015

Clinical

Skin

2016

Clinical

Skin

2016

In vivo

Skin

2017

Clinical

Skin

2019

Clinical

Skin

2022

Clinical

Joint

2009

Joint

2014

In vivo /In vitro
In vitro

Joint

2014

Clinical

Joint

2017

In vivo

Joint

2024

ClinicalJouin &Muscle

2019

Clinical

Bone

2014

In vitro

Bone

2017

In vitro

Bone2019

In vitro

Bone & Muscle

2017

ClinicalMuscle2016

Blood pressure

2009

In vivo /In vitro
In vivo

Blood vessel

2018

ClinicalPressure ulcer

2015

ClinicalPressure ulcer

2021

In vivo

Pressure ulcer

2021

In vivo

Diabetes

2016

In vivo

Liu C., et al. Absorption of hydroxyproline-containing peptides in vascularly perfused rat small intestine in situ.
Biosci. Biotech. Bioch.; 73:1741-1747, 2009
Sugihara F., et al. Quantification of hydroxyprolyl-glycine (Hyp-Gly) in human blood after ingestion of collagenhydrolysate. J Biosci. Bioeng.; 113:202-203, 2012
Osawa, Y., et al. Monitoring urinary collagen metabolite changes following collagen peptide ingestion and physicalactivity using ELISA with anti active collagen oligopeptide antibody. Sci Rep 11, 13527 (2021).
Sugihara F., et al. Clinical effects of collagen hydrolysates ingestion on UV-induced pigmented spots of human skin: A
preliminary study. Health Sciences; 28:153-156, 2012
Shimizu J., et al. Oral collagen-derived dipeptides, prolyl-hydroxyproline and hydroxyprolyl-glycine, ameliorate skinbarrier dysfunction and alter gene expression profiles in the skin. Biochem Biophys Res Commun. 9;456(2):626-30,
2014
Sugihara F., et al. Clinical effects of ingesting collagen hydrolysate on facial skin properties. Jpn. Pharmacol. Ther.;
43:67-70, 2015
Inoue N., et al. Ingestion of bioactive collagen hydrolysates enhance facial skin moisture and elasticity and reduce
facial ageing signs in a randomized double-blind placebo-controlled clinical study. J Sci Food Agric. 96(12):4077-81,
2016
Hyun-Jun Shin., et al. The Effect of Collagen Peptide Intake on UVB-induced Skin Damage in Hairless mice. Journalof the Korea Academia-Industrial cooperation Society;17(3): 611-621, 2016
Koizumi S., et al. Effects of Dietary Supplementation with Fish Scales-Derived Collagen Peptides on Skin Parameters
and Condition: A Randomized, Placebo-Controlled, Double-Blind Study; International Journal of Peptide Research
and Therapeutics, 1-6, 2017
Koizumi S., et al. The effects of collagen hydrolysates derived from tilapia scales or skin on human facial skin-arandomized Double-blind placebo controlled clinical study-, Japanese pharmacology and Therapeutics, vol. 47, no.1,
2019
Himeno, A., et al. Effect of Reducing Pigmentation by Collagen Peptide Intake: A Randomized, Double-Blind,
Placebo-Controlled Study. Dermatology and therapy, 2022
Nakatani S., et al. Chondroprotective effect of the bioactive peptide prolylhydroxyproline in mouse articular cartilage
in vitro and in vivo. Osteoarth. Cartilage; 17:1620-1627, 2009
Nakatani S., Transcriptome of ATDC5 Cultured with Glucosamine Hydrochloride and Collagen Hydrolysate Indicatesa New Candidate Gene for the Differentiation of Chondrocytes. J Chitin Chitosan Sci; 2:233-237, 2014
Kumar S., et al. Venkateswarathirukumara S: A double-blind, placebo-controlled, randomized, clinical study on theeffectiveness of collagen peptide on osteoarthritis. J Sci. Food Agric.; 95:702707, 2014
Isaka S., et al. Evaluation of the effect of oral administration of collagen peptides on an experimental rat osteoarthritis
model. EXPERIMENTAL AND THERAPEUTIC MEDICINE 13: 2699-2706, 2017
Devasia S., et al. Management and Amelioration of Knee Joint Osteoarthritis in Adults Using a Novel High-Functional
Bovine Collagen Peptide as a Nutritional Therapy: A Double-Blind, Prospective, Multicentric, Randomized, Activeand Placebo Controlled, Five-Arm, Clinical Study to Evaluate the Efficacy, Safety, and Tolerability. CARTILAGE.
0(0), 2024
Kimira Y., The effects of collagen peptide supplementation on knee joint health - a doble-blind, placebo-controlled,
randomized trial in healthy university students belonging to a running club-. Japanese pharmacology and Therapeutics,
47(9), 1455-1462, 2019
Kimira Y., et al. Collagen-derived dipeptide prolyl-hydroxyproline promotes differentiation of MC3T3-E1 osteoblasticcells. Biochem. Biophys. Res Co; 453:498-501, 2014
Kimira Y., et al. Collagen-derived dipeptide prolyl-hydroxyproline promotes osteogenic differentiation through Foxg1,Cellular & Molecular Biology Letters, 22:27, 2017
Nomura K., et al. Collagen-derived dipeptide prolyl hydroxyproline directly binds to Foxg1 to change its conformationand inhibit the interaction with Runx2, BIOSCIENCE,BIOTECHNOLOGY,ANDBIOCHEMISTRY, 2019
Kamada Y., et al. Effects of collagen peptide consumption on the muscle mass and osteo sono assessment index inyoung females, Annual Report of the Institute of Living and Environmental Sciences, 49, 2017
Kitakaze T., et al. The collagen derived dipeptide hydroxyprolyl-glycine promotes C2C12 myoblast differentiation andmyotube hypertrophy, Biochem Biophys Res Commun., 478(3):1292-7, 2016
Ichimura T., et al. Antihypertensive effect of enzymatic hydrolysate of collagen and Gly-Pro in spontaneously
hypertensive rats. Biosci. Biotech. Biochem., 73:2317-2319, 2009
Igase M., et al. A double-blind, placebo-controlled, randomised clinical study of the effect of pork collagen peptide
supplementation on atherosclerosis in healthy older individuals., Biosci. Biotech. Biochem., 2018 :1-3.
Sugihara F., et al. Collagen hydrolysate enhanced pressure ulcer healing in a randomized double-blind
placebo-controlled clinical study. Japanese pharmacology and Therapeutics, 43:1323-1328, 2015
Jimi S., et al. Collagen-derived dipeptide Pro-Hyp administration accelerates muscle regenerative healing accompanied
by less scarring after wounding on the abdominal wall in mice. Sci Rep 11, 18750, 2021
Jimi S., et al. A novel mouse wound model for scar tissue formation in abdominal muscle wall, Journal of Veterinary
Medical Science, 83(12):1933-1942, 2021
Iba Y., et al. Administration of Collagen Hydrolysates Improves Glucose Tolerance in Normal Mice ThroughGLP-1-Dependent and GLP-1-Independent Mechanisms, J Med Food., 19(9):836-43, 2016

June 2024

Collagen Peptide Technical Information
Papers related to Nitta Gelatin
FieldYear

SectionAuthor name, Title, Journal name

Diabetes

2018

ClinicalDiabetes

2019

ClinicalCognition

2019

ClinicalVisceral fat

2022

ClinicalVisceral fat

2022

In vitro

Inhibition
AGEs

2023

ClinicalOthers2020

In vitro

Devassia S., et al. Double Blind, Randomized Clinical Study to Evaluate Efficacy of Collagen Peptide as Add on
Nutritional Supplement in Type 2 Diabetes. ., Journal of Clinical Nutrition and Food Science, Vol.1, Issue 1-1002,2018Devasia S., et al. A Double Blind, Randomised, Four Arm Clinical Study to Evaluate the Safety, Efficacy andTolerability of Collagen Peptide as a Nutraceutical Therapy in the Management of Type II Diabetes Mellitus, JDiabetes Metab, Vol. 10 Iss. 11 No: 839, 2019
Koizumi S., et al. Effects of Collagen Hydrolysates on Human Brain Structure and Cognitive Function: A Pilot
Clinical Study, Nutrients 12, 50; doi:10.3390/nu12010050, 2020
Koizumi S., et al. Ingestion of Fermented Collagen Peptide Reduces Visceral Fat Mass: A Randomized Double-BlindPlacebo-Controlled Study, Japanese pharmacology and Therapeutics, Vol.50 (10): 1845-54: 2022.
Watanabe T., et al. Reduced Visceral Fat Weight and Body Weight Due to Ingestion of Fermented Collagen Peptide inHigh-Fat Diet-Fed Obese Mice, Journal of Nutritional Science and Vitaminology, 68(6): 533-539, 2022
Koizumi S., et al. Ingestion of a collagen peptide containing high concentrations of prolyl-hydroxyproline andhydroxyprolyl-glycine reduces advanced glycation end products levels in the skin and subcutaneous blood vessel
walls: a randomized, double-blind, placebo-controlled study, Bioscience, Biotechnology, and Biochemistry,87( 8):883-889, 2023
Asai TT., et al. Food-Derived Collagen Peptides, Prolyl-Hydroxyproline (Pro-Hyp), and Hydroxyprolyl-Glycine(Hyp-Gly) Enhance Growth of Primary Cultured Mouse Skin Fibroblast Using Fetal Bovine Serum Free from
Hydroxyprolyl Peptide. International Journal of Molecular Sciences. 21(1):229, 2020

June 2024

Collagen Peptide Technical Information
Patents of Nitta Gelatin
Patent No.

Title

Abstract

JP- 4490498
US-12/443,298,
13/523,438
CN-200880130932.0
CA-2732402
BE-08877173.8
DE-08877173.8
FN-08877173.8
UK-08877173.8
IN-2798/CHENP/2011
MY-P12011000459
SG-201100714-3
JP- 4523339

Disease suppressant (Bone,Joint, Pressure ulcer)

A peptide molecule body effective in suppressing various diseases such as osteoporosis,
osteoarthritis, and pressure ulcers, particularly a dipeptide that is easily absorbed into the body in theintestinal tract, and that contains the dipeptide as an essential dipeptide. A disease suppressing agent
containing a collagen peptide and the dipeptide as an essential active ingredient is provided. A
collagen peptide according to the present invention is characterized by containing a dipeptide having
a Hyp-Gly structure as an essential dipeptide. The dipeptide according to the present invention ischaracterized by having a Hyp-Gly structure. The disease suppressing agent according to the present
invention is characterized by containing a dipeptide having a Hyp-Gly structure as an essential activeingredient.

Materials for improving bone
toughness

JP- 4547015

Effervescent beverages andbeverage foaming agents

JP- 4709730

Chewable tablet

JP- 4904021

Collagen peptide-containing
cosmetic composition andmethod for producing thesame
Method for producing
degraded gelatin powder anddegraded gelatin powder

A material for improving bone toughness comprising, as an active ingredient, a peptide obtained byhydrolyzing collagen and/or gelatin with a protease derived from at least one selected from
Aspergillus yellow mold and bacteria of the genus Bacillus.
An effervescent drink containing saponin, collagen peptide having an average molecular weight of
20000 or less, and pectin contained in at least one selected from the group consisting of fruits andcitrus fruits.
A chewable tablet obtained by compressing a raw material powder mixture containing collagen
peptide in an amount of 25% by weight or more relative to the total amount, wherein the collagen
peptide has an average molecular weight of 4000 or less, and the N-terminal amino acid is occupied
by glycine. A chewable tablet characterized in that the proportion is greater than 65 mol %.
Collagen peptides with an average molecular weight of 200 to 1500 obtained by subcritical water
treatment under conditions of treatment temperature of 180 to 220°C, treatment pressure of 10 to 24
MPa, and treatment time of 30 to 120 minutes are used as cosmetic active ingredients. A cosmetic
composition containing collagen peptide.
Production of decomposed gelatin powder by hydrolyzing gelatin to obtain decomposed gelatin sothat the average molecular weight according to the Pagii method is 10000 to 30000, and then drying
and pulverizing the sol containing the decomposed gelatin without gelling.

JP- 5361155

JP-5612131
CA-2,825,157
CN-201280006535.9
US-13/981,258
TW-101102754

Therapeutic or prophylactic
agent for diabetes

JP- 5778692

Disease suppressant (Joint,bone and pressure ulcer
inhibitors by oligopeptides)
Whitening promoter andatopic dermatitis improving
agent

JP- 6100364

JP- 6240447

Elastin production promoter

JP-6407029
CN-201380022730.5
US-15/299172
JP- 6709440

Myoblast differentiation
promoterJP- 6877924

Epidermal intercellularfunction enhancer

June 2024

Composition for inhibiting
hypertrophic scar formation

Three or more selected from Glu-Hyp-Gly, Glu-Hyp, Leu-Hyp-Gly, Pro-Ala, Ser-Hyp, Ala-Hyp-Gly,chemical modifications thereof and pharmaceutically acceptable salts thereof containing collagen
peptide mixtures and Glu-Hyp-Gly, Glu-Hyp, Leu-Hyp-Gly, Pro-Ala, Ser-Hyp, Ala-Hyp-Gly,
Pro-Hyp-Gly, Leu-Hyp, Ile- At least one selected from the group consisting of Hyp, Ser-Hyp-Gly,
Gly-Pro-Hyp, (Pro-Hyp-Gly) 5, Pro-Hyp, Hyp-Gly, Pro-Gly, Pro-Pro and Ala-Hyp Peptides of thespecies, chemical modifications thereof, or pharmaceutically acceptable salts thereof have DPPIV
inhibitory activity and/or GLP-1 secretagogue activity, and are therefore effective as therapeutic or
preventive agents for diabetes.
p-Gly-Glu or Glu-Lys-Asp-Gly-His-Pro-Gly-Lys-Pro-Gly-Arg-A peptide consisting of an amino acidsequence represented by Hyp-Gly-Glu or a pharmaceutically acceptable salt thereof.
Hyp-Gly, Pro-Ala-Gly, Gly-Pro, Glu-Hyp-Gly, (Pro-Hyp-Gly) 5, (Pro-Hyp-Gly) 2, Pro-Hyp-Gly,Glu-Hyp, Ala- A peptide selected from the group consisting of Hyp-Gly, Ser-Hyp-Gly and Phe-Hyp
or a pharmaceutically acceptable salt thereof is useful as a whitening promoter or an atopic dermatitis
ameliorating agent.
An object of the present invention is to provide an elastin production promoter that is superior to theprior art and can prevent and improve wrinkles and sagging of the skin. [Solution] Glu-Hyp-Gly,
Ser-Hyp-Gly, Ala-Hyp-Gly, Glu-Hyp, Leu-Hyp-Gly, Ala-Hyp, Pro-Hyp-Gly, Leu-Hyp, Pro-Hyp, An
elastin production-enhancing agent comprising a peptide selected from the group consisting ofPro-Ala and Hyp-Gly or a pharmaceutically acceptable salt thereof.
A peptide selected from the group consisting of Ala-Hyp-Gly, Hyp-Gly-Pro, Leu-Hyp, Glu-Hyp,
Gly-Pro-Hyp, Pro-Ala, Hyp-Gly and Pro-Hyp or a pharmaceutically acceptable thereof the salt
obtained has a myoblast differentiation promoting effect superior to that of the prior art.
An object of the present invention is to provide a composition for inhibiting the formation of
hypertrophic scars. Kind Code: A1 A hypertrophic scar formation suppressing agent comprising atleast one polypeptide consisting of an amino acid sequence having a dipeptide sequence represented
by Pro-Hyp or Hyp-Gly, a chemical modification thereof, or a pharmaceutically acceptable salt
thereof. Composition.
Epidermal intercellular function-enhancing agent that enhances intercellular functions in theepidermis by containing a specific peptide. [Solution] The epidermal intercellular function enhancing
agent is Pro-Hyp, Hyp-Gly, Glu-Hyp, Gly-Pro, Pro-Hyp-Gly, (Pro-Hyp-Gly)2, Pro-Ala-Gly, Glu containing one or more peptides selected from the group consisting of Hyp-Gly, Ser-Hyp-Gly,
Pro-Ala, Phe-Hyp, Ala-Hyp and Ala-Hyp-Gly, derivatives thereof or salts thereof.