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Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection - PubMed

️Mon Jan 01 2024

Review

. 2024 Feb 27;29(5):1025.

doi: 10.3390/molecules29051025.

Zhiyong Liu^{1

2}, Junhong Gao^{1

2}, Yuhao Zhang^{1

2}, Hong Wang^{1

2}, Cunzhi Li^{1

2}, Xiaoqiang Lv^{1

2}, Yongchao Gao^{1

2}, Hui Deng^{1

2}, Bin Zhao^{1

2}, Ting Gao^{1

2}, Huan Li^{1

2}

Affiliations

PMID: 38474537
PMCID: PMC10934110
DOI: 10.3390/molecules29051025

Review

Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection

Xinying Peng et al. Molecules. 2024.

Abstract

Spider silk protein, renowned for its excellent mechanical properties, biodegradability, chemical stability, and low immune and inflammatory response activation, consists of a core domain with a repeat sequence and non-repeating sequences at the N-terminal and C-terminal. In this review, we focus on the relationship between the silk structure and its mechanical properties, exploring the potential applications of spider silk materials in the detection of energetic materials.

Keywords: biomaterials; biomedicine; spider silk; structural biology; structure.

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Conflict of interest statement

The authors declare no conflicts of interest.

Figures

**Figure 2**
Structural motifs and correlated secondary structures of spidroins [36]. (A) The variety of motifs in the repetitive domains of different spidroins directly reflect their mechanical properties, allowing them to perform different tasks. A: alanine, G: glycine, P: proline, Q: glutamine, S: serine, T: threonine; and X: one of tyrosine (Y); leucine (L); alanine, serine, and arginine (R); valine (V); or glutamine (Q). (B) Spider silk proteins (spidroins) are mainly composed of a repetitive domain (blue) flanked by the non-repetitive and highly conserved N-terminal (purple) and C-terminal (pink). Some specific types of spidroins have a linker region (yellow) and spacers (orange) in addition.

**Figure 1**
Schematic overview of silk produced by spider [9].

**Figure 3**
Molecular organization of spidroins with spacers. Spacer sequences were aligned using Jalview. Blue box in graphic represents GPGXX domain, green box represents GGX domain, gray box represents polyGA, and orange box represents spacer, the purple circle is N-terminal and pink circle is C-terminal. Sequences of spacer in MiSp are shaded in blue, and those in Flag are shaded in red. Gaps (-) indicate missing amino acid residues that have been inserted to align amino acid residues.

**Figure 4**
Schematic depictions of spider major ampullate silk gland and MaSp spidroin polypeptide chains [73]. Precursor spidroins, primarily adopting intrinsically disordered structures, can persist in a soluble state for long durations within the gland sac, serving as a concentrated liquid resource (silk dope). During the fiber creation process, spidroins traverse the serpentine spinning duct, undergoing extensive transformation. Conditions encountered in the duct include a pH shift (from neutral to acidic), an ion transition (from chaotropic to kosmotropic ions), dehydration, and the application of elongational and shear forces (due to the gradually narrowing duct structure). These collective circumstances trigger quick and precisely synchronized structural alterations in the distinct spidroin domains (N-terminal, repetitive domain, C-terminal), ultimately leading to the generation of large-scale silk fibers with a unique hierarchical arrangement.

**Figure 5**
Molecular organization of spidroins with linkers.

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Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection - PubMed

Influence of Spider Silk Protein Structure on Mechanical and Biological Properties for Energetic Material Detection

Abstract

Conflict of interest statement

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