In Vitro Analysis of the Co-Assembly of Type-I and Type-III Collagen
Küçük Resim Yok
Tarih
2017
Yazarlar
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
SPRINGER
Erişim Hakkı
info:eu-repo/semantics/openAccess
Özet
An important step towards achieving functional diversity of biomimetic surfaces is to better understand the co-assembly of the extracellular matrix components. For this, we study type-I and type-III collagen, the two major collagen types in the extracellular matrix. By using atomic force microscopy, custom image analysis, and kinetic modeling, we study their homotypic and heterotypic assembly. We find that the growth rate and thickness of heterotypic fibrils decrease as the fraction of type-III collagen increases, but the fibril nucleation rate is maximal at an intermediate fraction of type-III. This is because the more hydrophobic type-I collagen nucleates fast and grows in both longitudinal and lateral directions, whereas more hydrophilic type-III limits lateral growth of fibrils, driving more monomers to nucleate additional fibrils. This demonstrates that subtle differences in physico-chemical properties of similar molecules can be used to fine-tune their assembly behavior.
Açıklama
Anahtar Kelimeler
AFM, Biomimetic surface, Collagen, Extracellular matrix, Heterogeneous assembly, Macromolecular assembly
Kaynak
CELLULAR AND MOLECULAR BIOENGINEERING
WoS Q Değeri
Q3
Scopus Q Değeri
Q2
Cilt
10
Sayı
1
