Epidermal growth factor (EGF) is a protein containing 53 amino acids (R), that was first isolated from mice in the 1960s (R). It plays a pivotal role in wound healing and maintaining tissue integrity by regulating the survival, proliferation, migration, and differentiation of cells (R).
EGF has poor thermal stability, as the as the protein structure begins unfolding at 40°C (R). Reducing sugars also affect its stability, and polymers like poly(ethylene glycol) (PEG) and polysorbates increase its oxidation (R). EGF also has a short shelf life, remaining stable for only 3 months even under refrigeration (R).
The large size and hydrophilicity of EGF hinders its penetration of the skin barrier, necessitating the use of techniques to improve topical delivery, such as facial treatments, chemicals to disrupt the stratum corneum barrier, or encapsulation within particulate system or liposomes (R).
EGF is known to bind to EGF receptors on the cell membrane (R).
Outcome | Grade | Effect | Studies | |||||||
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Acne |
B
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Skin Oiliness |
B
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Fine Lines |
C
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Atrophic Scarring |
C
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Hyperpigmentation |
C
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Outcome | Effect | Frequency | Studies | |||||||
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Acne | ⇧ Increase |
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