Spidroin

Spidroin, N-terminal
Identifiers
SymbolSpidroin_N
PfamPF16763
InterProIPR031913
CATH2lpj
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Spidroin, C-terminal
Identifiers
SymbolSpidroin_MaSp
PfamPF11260
InterProIPR021001
CATH2m0m
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Spidroin-1
Identifiers
OrganismNephila clavipes
Symbol?
UniProtP19837
Search for
StructuresSwiss-model
DomainsInterPro
Spidroin-2
Identifiers
OrganismNephila clavipes
Symbol?
UniProtP46804
Search for
StructuresSwiss-model
DomainsInterPro
A diagram of the structure of spidroin

Spidroins are the main proteins in spider silk. Different types of spider silk contain different spidroins, all of which are members of a single protein family.[1] The most-researched type of spidroins are the major ampullate silk proteins (MaSp) used in the construction of dragline silk, the strongest type of spider silk. Dragline silk fiber was originally thought to be made up of two types of spidroins, spidroin-1 (MaSp1) and spidroin-2 (MaSp2) however recent transcriptomic analysis of over 1000 spider species has revealed multiple spidroins are expressed making it much more complex.[2][3][4]

Spidroin is part of a large group of proteins called scleroproteins. This group includes other insoluble structural proteins such as collagen and keratin.

A fiber of dragline spidroin is as thick and resistant as one of steel but is more flexible. It can be stretched to approximately 135% of its original length without breaking. Its properties make it an excellent candidate for use in various scientific fields.[5]

  1. ^ Cite error: The named reference acsp1 was invoked but never defined (see the help page).
  2. ^ Motriuk-Smith D, Smith A, Hayashi CY, Lewis RV (2005). "Analysis of the conserved N-terminal domains in major ampullate spider silk proteins". Biomacromolecules. 6 (6): 3152–9. doi:10.1021/bm050472b. PMID 16283740.
  3. ^ Moisenovich MM, Pustovalova O, Shackelford J, Vasiljeva TV, Druzhinina TV, Kamenchuk YA, et al. (May 2012). "Tissue regeneration in vivo within recombinant spidroin 1 scaffolds". Biomaterials. 33 (15): 3887–98. doi:10.1016/j.biomaterials.2012.02.013. PMID 22364702.
  4. ^ Arakawa K, Kono N, Malay AD, Tateishi A, Ifuku N, Masunaga H, et al. (October 2022). "1000 spider silkomes: Linking sequences to silk physical properties". Science Advances. 8 (41): eabo6043. Bibcode:2022SciA....8O6043A. doi:10.1126/sciadv.abo6043. PMC 9555773. PMID 36223455.
  5. ^ Askarieh G, Hedhammar M, Nordling K, Saenz A, Casals C, Rising A, et al. (May 2010). "Self-assembly of spider silk proteins is controlled by a pH-sensitive relay". Nature. 465 (7295): 236–8. Bibcode:2010Natur.465..236A. doi:10.1038/nature08962. PMID 20463740. S2CID 4366005.