On the roles of the alanine and serine in the β-sheet structure of fibroin

Mayen, Juan Francisco Carrascoza; Lupan, Alexandru; Cosar, Ciprian; Kun, Attila-Zsolt; Silaghi-Dumitrescu, Radu

doi:10.1016/j.bpc.2014.11.001

Cited by 13 publications

(7 citation statements)

References 31 publications

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“…Normally, in fibrillar protein structural studies, hydrogen bonds are the most important stabilizing agents in biomaterials, such as silk, collagen, and amyloid proteins, which act like chemical glue. 33 Our calculated number of hydrogen bonds between spider and silkworm fibroins showed similar results as those observed from previous DFT studies by Mayen et al 26 From their results, the inclusion of a serine residue lowered the stabilizing energies and the number of hydrogen bonds to a greater extent than did (Gly) n and (Gly-Ala) n composition. In addition, computational studies involving spider silk materials by Keten et al 21,22 and Cheng et al, 24 reported that hydrogen bonding was the source of the considerable mechanistic behaviors observed in spider silk and its fibroin structures.…”

Section: Discussionsupporting

confidence: 88%

“…N. clavipes, Argiope aurantia, Nephila cruentata, Parawixla audax, Argiope argentat, and Antheraea fibers), although the protein was regarded as silkworm fibroin structures. 9,13,16 In a similar manner, structural differences in the atomistic scale between spider and silkworm fibroin segments were investigated by Mayen et al 26 Mayen et al investigated the effect of alanine and serine residues in b-sheets of backbone silk structures with solvent interaction using density function theory (DFT) and the MD study. 26 Through the DFT and MD study, different mechanical characteristics were observed to be induced by the backbone residue sequences: Gly-Ala-Gly-Ala-Gly-Ala-Gly (GAGAGAG) and Gly-Ala-Gly-Ala-Gly-Ala-Ser (GAGAGAS) repeats in spider and silkworm silk fibroin, respectively.…”

Section: Introductionmentioning

confidence: 99%

“…9,13,16 In a similar manner, structural differences in the atomistic scale between spider and silkworm fibroin segments were investigated by Mayen et al 26 Mayen et al investigated the effect of alanine and serine residues in b-sheets of backbone silk structures with solvent interaction using density function theory (DFT) and the MD study. 26 Through the DFT and MD study, different mechanical characteristics were observed to be induced by the backbone residue sequences: Gly-Ala-Gly-Ala-Gly-Ala-Gly (GAGAGAG) and Gly-Ala-Gly-Ala-Gly-Ala-Ser (GAGAGAS) repeats in spider and silkworm silk fibroin, respectively. Furthermore, they analyzed the various stabilization energies and hydrogen bonds associated with (Gly) n , (GlyAla) n , and (GlySer) n compositions.…”

Section: Introductionmentioning

confidence: 99%

“…Furthermore, they analyzed the various stabilization energies and hydrogen bonds associated with (Gly) n , (GlyAla) n , and (GlySer) n compositions. 26 From their results, stable stabilization energies were calculated and the number of hydrogen bonds involved with the (GlySer) n sequence was observed relative to that of (Gly) n and (GlyAla) n sequences. Based on experimental studies at the nano scale and the DFT study at the atomistic scale, it was found that the b-sheet crystalline lattice associated with of the silkworm silk protein including serine residues was more stable and exhibited additional mechanical characteristics as compared to spider silk proteins.…”

Section: Introductionmentioning

confidence: 99%

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Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Lee

Kwon

2016

Phys. Chem. Chem. Phys.

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Spider and silkworm silk proteins have received much attention owing to their inherent structural stability, biodegradability, and biocompatibility. These silk protein materials have various mechanical characteristics such as elastic modulus, ultimate strength and fracture toughness. While the considerable mechanical characteristics of the core crystalline regions of spider silk proteins at the atomistic scale have been investigated through several experimental techniques and computational studies, there is a lack of comparison between spider and silkworm fibroins in the atomistic scale. In this study, we investigated the differences between the mechanical characteristics of spider and silkworm fibroin structures by applying molecular dynamics and steered molecular dynamics. We found that serine amino acids in silkworm fibroins not only increased the number of hydrogen bonds, but also altered their structural characteristics and mechanical properties.

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Section: Discussionsupporting

confidence: 88%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Lee

Kwon

2016

Phys. Chem. Chem. Phys.

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“…The sequence of amino acids influences the structural properties of fibroin [17,24,35]. In silk II, alanine and serine affect the rigidity of β-sheets; alanine provides stability to the sheets, whereas serine is responsible for hydrophobicity [36]. A recent study of the differences in the structural characteristics and properties of cocoons produced by varieties of B. mori concluded that the molecular weight of regenerated SF, viscosity in solution, and mechanical properties depended on the variety of the silkworm [37]; however, months later, Jang et al [38] reported that the differences observed in mechanical properties could be attributed to the techniques used to measure them, such as wet spinnability [38].…”

Section: Rdms000740 10(3)2019mentioning

confidence: 99%

Scaffolds Based on Silk Fibroin for Osteochondral Tissue Engineering

Moncada‐Saucedo

Camacho‐Morales

Fuentes-Mera

2019

RDMS

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Physical and chemical features of silk fibroin as a biomaterialSFs from the cocoons of the silkworm B. mori are the most-used and most-studied SFs in TE; South Korea is home to over 300 varieties of this species [16]. Silkworm cocoons primarily consist of 2 bio-macromolecules: fibroin (fibrous protein) and sericin (globular protein). The silk of B. mori is synthesized in a group of specialized salivary glands, and fibroin (comprising 60-80% of the silk) is synthesized exclusively in the posterior region of the gland. The fibroin fibres are covered with sericin (15-35%), which is synthesized in the walls of the medial regions of the gland. Between 1 and 5% of the silk consists of non-sericin components, such as pigments, wax, sugars, and other impurities (Figure 1), [1,17,18].Most lepidopterans produce fibroin that consists of 3 protein components arranged as a single element of silk: heavy-chain (~391kDa) and light-chain fibroins (~25kDa), which are linked by a disulphide bridge, and P25 (~25kDa), also known as fibrohexamerin (Fhx), These components are present at a 6:6:1 ratio, respectively [19][20][21].

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The Effect of Assam Silk Fibroin on the Bacterial Cellulose Cytocompatibility as the Extracellular Matrix

Mahendra,

Astuti

2024

Starch Stärke

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The growing interest in natural polymers for biomedical and tissue engineering has fueled the search for materials with superior mechanical and biological properties. Bacterial cellulose (BC) and silk fibroin (SF) emerge as promising candidates meeting these criteria. This study focuses on enhancing BC through high‐pressure homogenization (HPH) and subsequent functionalization with Assam silk fibroin (ASF) using an ex‐situ approach. Analysis via attenuated total reflection–Fourier transform infrared (ATR–FTIR) spectroscopy confirms the successful integration of ASF into the HPH‐treated BC scaffold. The diffractogram of HPH‐BC/ASF indicates the prevalence of type I cellulose crystalline structures, with variations in lamellar and porous architecture based on component ratios. Mechanical testing, particularly the compressive test, reveals that the HPH‐BC/ASF formulation exhibits the highest compressive stress and modulus compared to other samples. Supplementary analyses, including swelling ratio and porosity measurements, support the superior compressive properties of HPH‐BC/ASF. Moreover, the cell viability of chondrocytes demonstrates compatibility with the BC‐based scaffold material. These findings underscore the potential applications of HPH‐BC and ASF in areas such as scaffolding for the development of extracellular matrix.

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On the roles of the alanine and serine in the β-sheet structure of fibroin

Cited by 13 publications

References 31 publications

Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Mechanical behavior comparison of spider and silkworm silks using molecular dynamics at atomic scale

Scaffolds Based on Silk Fibroin for Osteochondral Tissue Engineering

The Effect of Assam Silk Fibroin on the Bacterial Cellulose Cytocompatibility as the Extracellular Matrix

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