Hydroxyproline is a component of collagen and is essential for its stability. It is formed by the hydroxylation of proline. It helps provide stability to the triple-helical structure of collagen by forming hydrogen bonds. It is involved in various biological processes related to connective tissue.

L-hydroxyproline, also known as Trans-4-hydroxy-L-proline or Trans-Hyp, is extensively utilized in the food, cosmetic, biochemistry, medical, and other industries. Furthermore, it has been discovered that several secondary metabolites, like actinomycins and echinocandins, include L-hydroxyproline. Because it is abundant in collagen, L-hydroxyproline is mostly produced industrially by acid hydrolyzing mammalian collagen[1].
Hydroxyproline is a major component of the protein collagen. It plays a key role in collagen stability. It permits the sharp twisting of the collagen helix. It helps provide stability to the triple-helical structure of collagen by forming hydrogen bonds.

Hydroxyproline is used as a skin-conditioning amino acid. It is a component of collagen and is essential for maintaining the stability of the collagen helix. It is involved in the structure and function of connective tissues.

Hydroxyproline is evaluated in cell-free assays for its ability to stabilize collagen structure. However, specific enzymatic or receptor binding assays are not well-documented. Its role in collagen stability can be studied using biochemical and biophysical methods.

Hydroxyproline is assessed in cell-based assays to study its role in collagen synthesis and stability. Cells that produce collagen, such as fibroblasts, are treated with Hydroxyproline, and collagen production and stability are measured.

Hydroxyproline is administered in animal models to study its effects on collagen synthesis and connective tissue health. However, specific animal study protocols are not extensively documented. It is a component of collagen and is involved in various physiological processes.

Hydroxyproline has a molecular weight of 131.13 and a molecular formula of C5H9NO3. It has a CAS number of 51-35-4. The compound is a white crystalline powder. It is soluble in water.

No detailed toxicity data is available for Hydroxyproline. The compound is a naturally occurring amino acid and is generally considered safe. It is used in research and cosmetic applications.

[1]. Biosynthesis of trans-4-hydroxyproline by recombinant strains of Corynebacterium glutamicum and Escherichia coli. BMC Biotechnol. 2014 May 19;14:44.

Trans-4-hydroxy-L-proline is an optically active form of 4-hydroxyproline, exhibiting the L-trans configuration. It is found in humans, plants, and mice, and is a zwitterion tautomer of trans-4-hydroxy-L-proline. Hydroxyproline is a neutral heterocyclic protein amino acid found in collagen and is therefore commonly found in many gelatin products. Hydroxyproline is primarily used as a diagnostic marker for bone turnover and liver fibrosis. In terms of treatment, hydroxyproline is being investigated as an experimental drug, but it has been approved in France for the treatment of small, superficial wounds, in a compound topical gel product called Cicactive. Hydroxyproline is a metabolite found in or produced by Escherichia coli (K12 strain, MG1655 strain). 4-Hydroxy-L-proline is a metabolite found in or produced by Escherichia coli (K12 strain, MG1655 strain). Hydroxyproline has been reported in Daphnia pulex, Glycine max, and other organisms with relevant data. Hydroxyproline is a non-essential amino acid derivative formed during post-translational modification of proteins by the hydroxylation of the amino acid proline by prolyl hydroxylase, an enzyme that requires vitamin C as a cofactor. Hydroxyproline is a major component of collagen and plays a crucial role in maintaining the stability of the collagen triple helix structure. Hydroxyproline can be used as an indicator of collagen content. Elevated levels of hydroxyproline in urine and/or serum are often associated with connective tissue degradation. Vitamin C deficiency reduces the conversion of proline to hydroxyproline, leading to decreased collagen stability. 4-Hydroxyproline (or hydroxyproline or Hyp) is a major component of collagen. Hydroxyproline is generated by the hydroxylation of the amino acid proline, and is therefore a post-translational modified amino acid. Hydroxyproline and proline play crucial roles in maintaining collagen stability. In particular, they can cause significant distortion of the collagen helix. Hydroxyproline is rarely found in other proteins besides collagen. The only protein in mammals containing hydroxyproline is elastin. Therefore, hydroxyproline content has been used as an indicator of collagen and/or gelatin content in tissue or biological samples. Serum and urine hydroxyproline levels are elevated in patients with Paget's disease. Hydroxyproline (Hyp) content in bodily fluids has been used as an indicator of collagen catabolism, particularly related to bone resorption or tissue degradation. Serum hydroxyproline levels are significantly higher in bedridden and elderly individuals than in normally active individuals. Elevated urinary hydroxyproline levels also suggest muscle damage. Increased reactive oxygen species (ROS) are known to accelerate collagen degradation. Hydroxyproline levels are also elevated under conditions of depression and stress (A3486, A3487, A3488, A3489). See also: Hydroxyproline; Octyl methoxycinnamate (ingredient); Hydroxyproline; Nicotinamide (ingredient)... See more...

---

Drug Indications
In France, this product is used as a compound preparation for the treatment of small, superficial wounds.

---

Pharmacodynamics
Hydroxyproline, along with proline and glycine, are major components of collagen. Collagen is one of the main components of connective tissues such as skin, bones, and cartilage. Therefore, when these tissues are damaged, hydroxyproline is essential for repairing damaged areas.
Hydroxyproline is a non-standard amino acid primarily found in collagen. It has a CAS number of 51-35-4. It plays a critical role in stabilizing the triple-helix structure of collagen. It is used in research to study collagen structure and function. It is a naturally occurring compound.

C5H9NO3

131.13

131.058

51-35-4

25249-07-4

5810

White to off-white solid powder

1.4±0.1 g/cm3

355.2±42.0 °C at 760 mmHg

273 °C (dec.)(lit.)

168.6±27.9 °C

0.0±1.8 mmHg at 25°C

1.540

-1.84

3

4

1

9

125

2

O([H])C1([H])C([H])([H])N([H])[C@]([H])(C(=O)O[H])C1([H])[H]

PMMYEEVYMWASQN-DMTCNVIQSA-N

InChI=1S/C5H9NO3/c7-3-1-4(5(8)9)6-2-3/h3-4,6-7H,1-2H2,(H,8,9)/t3-,4+/m1/s1

(2S,4R)-4-hydroxypyrrolidine-2-carboxylic acid

NSC 46704; Oxaceprol; Hydroxyproline

2934.99.9001

Powder      -20°C    3 years

                     4°C     2 years

In solvent   -80°C    6 months

                  -20°C    1 month

Room temperature (This product is stable at ambient temperature for a few days during ordinary shipping and time spent in Customs)

H2O : ~50 mg/mL (~381.30 mM)

Solubility in Formulation 1: 100 mg/mL (762.60 mM) in PBS (add these co-solvents sequentially from left to right, and one by one), clear solution; with sonication.

---

 (Please use freshly prepared in vivo formulations for optimal results.)