BACKGROUND: This pilot study investigated the effects of a 12-week administration of a nutritional supplement containing special collagen peptides on the structural and molecular properties of the collagen fiber network in the human skin. For the assessments, the suction blister method and electron microscopical comparisons were used.
METHODS: Three suction blisters were generated on the inner forearm of each test subject before and after the 12-week administration of the nutritional supplement. High-resolution scanning electron microscopy (SEM) was employed to meticulously investigate the structural characteristics of the skin\'s collagen network, including the length and diameter of collagen fibers within the suction blister roof. Furthermore, the analysis included immunohistochemistry and fluorescence light microscopy to study hyaluronic acid within the extracellular matrix. Additional assessments encompassed changes in various epidermal parameters. Nine female participants within the age range of 43.7-61.8 years (mean: 52.5 ± 5.9 years) completed the study in accordance with the study protocol.
RESULTS: Compared with baseline, the 12-week supplementation regimen led to a statistically significant average increase in the collagen fiber network size of 34.56% (p < 0.0001). Additionally, collagen fiber cross-linking and fiber length were substantially increased. The ingestion of the supplement also resulted in an 18.08% elevation in epidermal hyaluronic acid concentration (p < 0.0001). No adverse events were recorded during the study.
CONCLUSIONS: Using an innovative approach, this study demonstrated the ability of a targeted nutritional supplement to effectively restore the ultrastructural integrity of the dermal collagen network, which is typically disrupted by the natural aging process of the skin. These findings not only corroborate existing data regarding the positive effects of oral collagen peptides on skin structure and function but also contribute to our understanding of ultrastructural morphological aspects of changes in the skin\'s collagen network. Supplementation can induce regeneration of the collagen fiber network in the human skin.
BACKGROUND: German Clinical Trials Register, DRKS-ID DRKS00034161- Date of registration: 06.05.2024, retrospectively registered.
Is it possible to improve the structure and molecular properties of the collagen fiber network in human skin by taking collagen peptides orally? To find out, suction blisters were created on the inner forearm of nine women before and after taking a nutritional supplement containing special collagen peptides for 12 weeks. To detect changes in the collagen fiber network, the inner surfaces of the roofs of the isolated suction blisters were examined using scanning electron microscopy. Additionally, hyaluronic acid levels were measured with fluorescence light microscopy. As a result, it was shown for the first time that a 12-weeks supplement regimen can lead to a statistically significant increase in the size of the collagen fiber network. Moreover, collagen fiber cross-linking and fiber length were substantially increased. The supplement also led to a statistically significant rise in epidermal hyaluronic acid levels. These findings not only support existing data on the positive effects of oral collagen peptides on skin structure and function but also enhance our understanding of the detailed morphological changes in the skin’s collagen network.

BACKGROUND: A healthy skin provides protection against intrinsic and extrinsic factors. Skin aging is characterized by structural and morphological alterations affecting skin health, integrity, and functionality, resulting in visible aging signs.
OBJECTIVE: The primary objective of this study was to assess the effect of a collagen peptide dietary supplement on skin aging in the East Asian population.
METHODS: Eighty-five healthy women, aged from 43 to 65 years old, were randomly assigned to the collagen supplement (CP, 5 g) or placebo (maltodextrin, 5 g) group. To standardize daily skin care, the volunteers in both groups used a specific face cream for 28 days prior to and throughout the supplementation period, creating an equal baseline for the assessment of the efficacy of CP on several skin parameters. At baseline, day 28 and day 84, the following hallmarks of skin and nail aging were assessed: dermis density, skin moisture and elasticity, wrinkle visibility, beauty perception, and nail color.
RESULTS: After 84 days, a significant improvement of dermis density and skin moisture was observed in the collagen peptides group compared to the placebo group. Positive effects on skin elasticity, wrinkle visibility, nail color, and overall beauty perception were already observed within 28 days of supplementation in the CP group, while the same effects in the placebo group were only observed after 84 days.
CONCLUSIONS: Taken together, these results show that, in addition to a standardized skin care, daily supplementation with 5 g of collagen peptides positively affects visible signs of skin and nail aging in the East Asian population.

BACKGROUND: Collagen peptides from various sources demonstrate benefits in health and well-being both in vitro and in clinical trials. However, there is a scarce study of collagen peptides from Tuna on skin health.
OBJECTIVE: To investigate the impact of collagen peptides derived from Tuna (Katsuwonus pelamis and Thunnus albacares) on skin health, utilizing in vitro biological studies and a randomized controlled trial.
METHODS: In vitro biological studies on human dermal primary fibroblasts were evaluated in terms of collagen and elastin synthesis and senescent cell inhibition. A randomized, placebo-controlled, double-blind clinical trial was conducted on 72 women who were randomly assigned to receive either tuna collagen peptides (n = 36) or a placebo (n = 36) orally for 8 weeks and 2 weeks post-ingestion by measuring skin hydration, transepidermal water loss (TEWL), skin elasticity, and skin density.
RESULTS: In vitro biological effects demonstrated dose-dependent positive results in increasing collagen and elastin synthesis and reducing senescent cells. The effects on collagen and senescent cells plateaued at high concentrations. A clinical trial showed that the test group experienced a significant increase in skin hydration, elasticity, and density, along with a decrease in TEWL compared to the baseline. The test and placebo groups showed statistically significant differences at 8 weeks for all parameters except for the TEWL at the face. All positive effects were substantially retained even after 2 weeks of discontinuation.
CONCLUSIONS: These findings demonstrate the significant potential of tuna collagen peptides to promote human skin health, warranting further investigation as a potential nutraceutical.

The intake of specific collagen peptides (SCPs) has been shown to decrease activity-related knee pain in young, physically active adults. This trial investigated the effect of a 12-week SCP supplementation in a wider age range of healthy men and women over 18 years with functional knee and hip pain during daily activities. A total of 182 participants were randomly assigned to receive either 5 g of specific collagen peptides (CP-G) or a placebo (P-G). Pain at rest and during various daily activities were assessed at baseline and after 12 weeks by a physician and participants using a 10-point numeric rating scale (NRS). The intake of 5 g SCP over 12 weeks significantly reduced pain at rest (p = 0.018) and during walking (p = 0.032) according to the physician\'s evaluation. Participants in the CP-G also reported significantly less pain when climbing stairs (p = 0.040) and when kneeling down (p < 0.001) compared to the P-G. Additionally, after 12 weeks, restrictions when squatting were significantly lower in the CP-G compared with the P-G (p = 0.014). The daily intake of 5 g of SCP seems to benefit healthy adults with hip and knee joint discomforts by reducing pain during daily activities.

A new extracellular protease from Bacillus subtilis strain MPK with collagenolytic activity was isolated and purified. Fish skin which otherwise would be treated as waste is used as substrate for the production of protease. Using various techniques such as ammonium sulphate precipitation and ion exchange chromatography, protease was purified and characterized subsequently. Protease of approximately 61 kDa molecular weight was purified by 135.7-fold with 18.42% enzyme recovery. The protease showed effective properties like pH and temperature stability over a broad range with optimum pH 7.5 and temperature 60 °C. Km and Vmax were found to be 1.92 mg ml-1 and 1.02 × 10-4 mol L-1 min-1, respectively. The protease exhibited stability in various ions, surfactants, inhibitors and organic solvents. Subsequently, the protease was successfully utilized for collagen hydrolysis to generate collagen peptides; thus, the produced protease would be a potential candidate for multifaceted applications in food and pharmaceutical industries due to its significant characteristics and collagenolytic properties.

UNASSIGNED: Collagen peptide supplementation in conjunction with exercise has been shown to improve structural and functional adaptations of both muscles and the extracellular matrix. This study aimed to explore whether specific collagen peptide (SCP) supplementation combined with a concurrent training intervention can improve muscular stress after exercise-induced muscle damage, verified by reliable blood markers.
UNASSIGNED: 55 sedentary to moderately active males participating in a concurrent training (CT) intervention (3x/week) for 12 weeks were administered either 15 g of SCP or placebo (PLA) daily. Before (T1) and after the intervention (T2), 150 muscle-damaging drop jumps were performed. Blood samples were collected to measure creatine kinase (CK), lactate dehydrogenase (LDH), myoglobin (MYO) and high-sensitivity C-reactive protein (hsCRP) before, after, and at 2 h, 24 h and 48 h post exercise.
UNASSIGNED: A combination of concurrent training and SCP administration showed statistically significant interaction effects, implying a lower increase in the area under the curve (AUC) of MYO (p = 0.004, ηp2 = 0.184), CK (p = 0.01, ηp2 = 0.145) and LDH (p = 0.016, ηp2 = 0.133) in the SCP group. On closer examination, the absolute mean differences (ΔAUCs) showed statistical significance in MYO (p = 0.017, d = 0.771), CK (p = 0.039, d = 0.633) and LDH (p = 0.016, d = 0.764) by SCP supplementation.
UNASSIGNED: In conclusion, 12 weeks of 15 g SCP supplementation combined with CT intervention reduced acute markers of exercise-induced muscle damage and improved post-exercise regenerative capacity, as evidenced by the altered post-exercise time course. The current findings indicate that SCP supplementation had a positive effect on the early phase of muscular recovery by either improving the structural integrity of the muscle and extracellular matrix during the training period or by accelerating membrane and cytoskeletal protein repair.
UNASSIGNED: https://www.clinicaltrials.gov/study/NCT05220371?cond=NCT05220371&rank=1, NCT05220371.

Facial masks have become ubiquitous in our daily life to endow skin enough moisture and activated nutrition through mask nonwovens infused with skincare ingredients. However, the active nutrients in wet masks are prone to deterioration and deactivation. Herein, a novel multifunctional nanofiber dry mask was successfully prepared using aqueous-electrospun phenolic acid grafted chitosan/collagen peptides. When used, the functional nanofibers in the mask dissolve through spraying moisture, activating active ingredients in response to water and providing in-situ free radical scavenging, moisturizing and antibacterial effects to the skin. In this work, a series of gallic acid (GA), caffeic acid (CA), and protocatechuic acid (PA) have been studied to be grafted with chitosan to improve water solubility of chitosan (CS). Also, through aqueous electrospinning of phenolic acid-grafted chitosan/collagen peptides, a one-step green multifunctional nanofiber mask was obtained. The results showed that the mask had a 12.14 % moisturizing rate and a 94.09 % activity for removing free radicals from the skin after encountering moisture. Considering its high efficiency, controllable function release, and easy processability, the nanofiber multifunctional mask may provide a competitive alternative to facial masks and promote potential value-added applications of bio-based macro-molecules.

Chronic non-healing cutaneous wounds represent a major burden to patients and healthcare providers worldwide, emphasising the continued unmet need for credible and efficacious therapeutic approaches for wound healing. We have recently shown the potential for collagen peptides to promote proliferation and migration during cutaneous wound healing. In the present study, we demonstrate that the application of porcine-derived collagen peptides significantly increases keratinocyte and dermal fibroblast expression of integrin α2β1 and activation of an extracellular signal-related kinase (ERK)-focal adhesion kinase (FAK) signalling cascade during wound closure in vitro. SiRNA-mediated knockdown of integrin β1 impaired porcine-derived collagen peptide-induced wound closure and activation of ERK-FAK signalling in keratinocytes but did not impair ERK or FAK signalling in dermal fibroblasts, implying the activation of differing downstream signalling pathways. Studies in ex vivo human 3D skin equivalents subjected to punch biopsy-induced wounding confirmed the ability of porcine-derived collagen peptides to promote wound closure by enhancing re-epithelialisation. Collectively, these data highlight the translational and clinical potential for porcine-derived collagen peptides as a viable therapeutic approach to promote re-epithelialisation of superficial cutaneous wounds.

Antioxidant peptides are currently a hotspot in food science, pharmaceuticals, and cosmetics. In different fields, the screening, activity evaluation, mechanisms, and applications of antioxidant peptides are the pivotal areas of research. Among these topics, the efficient screening of antioxidant peptides stands at the forefront of cutting-edge research. To this end, efficient screening with novel technologies has significantly accelerated the research process, gradually replacing the traditional approach. After the novel antioxidant peptides are screened and identified, a time-consuming activity evaluation is another indispensable procedure, especially in in vivo models. Cellular and rodent models have been widely used for activity evaluation, whilst non-rodent models provide an efficient solution, even with the potential for high-throughput screening. Meanwhile, further research of molecular mechanisms can elucidate the essence underlying the activity, which is related to several signaling pathways, including Keap1-Nrf2/ARE, mitochondria-dependent apoptosis, TGF-β/SMAD, AMPK/SIRT1/PGC-1α, PI3K/Akt/mTOR, and NF-κB. Last but not least, antioxidant peptides have broad applications in food manufacture, therapy, and the cosmetics industry, which requires a systematic review. This review introduces novel technologies for the efficient screening of antioxidant peptides, categorized with a new vision. A wide range of activity evaluation assays, encompassing cellular models, as well as rodent and non-rodent models, are provided in a comprehensive manner. In addition, recent advances in molecular mechanisms are analyzed with specific cases. Finally, the applications of antioxidant peptides in food production, therapy, and cosmetics are systematically reviewed.

Collagen peptides exhibit various bioactivities, including antioxidation and ACE inhibition. However, the bioactivities of collagen peptides decrease gradually due to oxidation deterioration during storage, and this degradation of bioactive peptides is rarely studied. In this study, the oxidative levels and the bioactivities of collagen peptides were investigated during an oxidative-induced storage accelerated by lipids. The results suggested that the oxidation of collagen peptides was divided into three stages. At the early stage, the carbonyl content of collagen peptides increased rapidly (from 2.32 to 3.72 μmol/g peptide), showing a close correlation with their bioactivities (for antioxidation, r = -0.947; for ACE inhibition, r = -0.911). The oxidation level in the middle stage continued but was stable, and the bioactivities decreased. At the later stage, the Schiff base and dityrosine content increased significantly and showed a strong correlation with the bioactivities (antioxidation, r = -0.820, -0.801; ACE inhibition, r = -0.779, -0.865). The amino acid and proteomic analyses showed that Met, Lys, and Arg were susceptible to oxidation and revealed their oxidative modification types. This study provided an insight into the dynamic oxidative modifications of collagen peptides, which were shown to correlate well with the change in bioactivities.