Study on the Formation of Amyloid Fibrils by Self-assembly of an Artificially Designed Peptide GAV-6_Journal of Biomedical Engineering

Authors：

ZHANGJie ¹ , TANGChengkang ² , CHENYongzhu ³ , XINGZhihua ² ,  QIUFeng ²

1. Key Lab of Transplant Engineering and Immunology, Ministry of Health, West China Hospital, Sichuan University, Chengdu 610041, China;
2. Regenerative Medicine Research Center, West China Hospital, Sichuan University, Chengdu 610041, China;
3. Periodical Press of West China Hospital, Sichuan University, Chengdu 610041, China;

Corresponding author：

QIUFeng, Email: fengqiu@scu.edu.cn

Keywords：

peptide; self-assembly; amyloid fibrils; micelle

DOI：

10.7507/1001-5515.20140128

Video：

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Abstract Full text Figures/Tables Video References Cited by

Amyloid fibrils belong to a category of abnormal aggregations of natural proteins, which are closely related to many human diseases. Recently, some critical peptide sequences have been extensively studied for clarifying the molecular mechanism of natural proteins to form amyloid fibrils. In the present study, we designed a short peptide GGAAVV (GAV-6) composed of hydrophobic amino acids glycine (G), alanine (A) and valine (V) and studied its ability to form amyloid fibrils. As characterized by atomic force microscopy (AFM) and dynamic light scattering (DLS), the peptide could self-assemble into smooth nanofibers without branches. Congo red staining/binding and thioflavin-T (ThT) binding experiments show that the nanofibers formed by GAV-6 shared identical properties with typical amyloid fibrils. These results show that the designed peptide GAV-6 could self-assemble into typical amyloid fibrils, which might make it a useful model molecule to clarify the mechanism for the formation of amyloid fibrils in the future.

Citation： ZHANGJie, TANGChengkang, CHENYongzhu, XINGZhihua, QIUFeng. Study on the Formation of Amyloid Fibrils by Self-assembly of an Artificially Designed Peptide GAV-6. Journal of Biomedical Engineering, 2014, 31(3): 686-690. doi: 10.7507/1001-5515.20140128 Copy

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9.	CHEN Y, QIU F, LU Y, et al. Geometrical shape of hydrophobic section determines the self-assembling structures of peptide detergents and bolaamphiphilic peptides[J]. Curr Nanosci, 2009, 5(1):69-74.
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12.	DESAI H V, ARONOW W S, PETERSON S J, et al. Cardiac amyloidosis:approaches to diagnosis and management[J]. Cardiol Rev, 2010, 18(1):1-11.
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14.	RAMSHINI H, PARRINI C, RELINI A, et al. Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils[J]. PLoS One, 2011,6(1):e16075.
15.	PALMIERI L C, MELO-FERREIRA B, BRAGA CA, et al. Stepwise oligomerization of murine amylin and assembly of amyloid fibrils[J]. Biophys Chem, 2013, 180-181:135-144.
16.	LEMBRÉ P, VENDRELY C, DI MARTINO P. Amyloid fiber formation by synthetic peptides derived from the sequence of the protein CsgA of Escherichia coli[J]. Protein Pept Lett, 2013, 20(8):942-946.

1. MAKIN O S, SERPELL L C. Structures for amyloid fibrils[J]. Febs J, 2005, 272(23):5950-5961.
2. GOTO Y, YAGI H, YAMAGUCHI K, et al. Structure, formation and propagation of amyloid fibrils[J]. Curr Pharm Des, 2008,14(30):3205-3218.
3. NORLIN N, HELLBERG M, FILIPPOV A, et al. Aggregation and fibril morphology of the Arctic mutation of Alzheimer's Aβ peptide by CD, TEM, STEM and in situ AFM[J]. J Struct Biol, 2012,180(1):174-189.
4. TAO K, WANG J, ZHOU P, et al. Self-assembly of short Aβ(16-22) peptides:effect of terminal capping and the role of electrostatic interaction[J]. Langmuir, 2011, 27(6), 2723-2730.
5. ZIBAEE S, FRASER G, JAKES R, et al. Human beta-synuclein rendered fibrillogenic by designed mutations[J]. J Biol Chem,2010, 285(49):38555-38567.
6. PILLAY K, GOVENDER P. Amylin uncovered:a review on the polypeptide responsible for type Ⅱ diabetes[J]. Biomed Res Int,2013, 2013:826706.
7. LIU J, ZHAO X. Design of self-assembling peptides and their biomedical applications[J]. Nanomedicine, 2011, 6(9):1621-1643.
8. ZHAO X, PAN F, XU H, et al. Molecular self-assembly and applications of designer peptide amphiphiles[J]. Chem Soc Rev, 2010, 39(9), 3480-3498.
9. CHEN Y, QIU F, LU Y, et al. Geometrical shape of hydrophobic section determines the self-assembling structures of peptide detergents and bolaamphiphilic peptides[J]. Curr Nanosci, 2009, 5(1):69-74.
10. QIU F, CHEN Y, TANG C, et al. De novo design of a bolaamphiphilic peptide with only natural amino acids[J]. Macromol Biosci, 2008, 8(11):1053-1059.
11. HOU L, LEE H G, HAN F, et al. Modification of amyloid-β1-42 fibril structure by methionine-35 oxidation[J]. J Alzheimers Dis,2013, 37(1):9-18.
12. DESAI H V, ARONOW W S, PETERSON S J, et al. Cardiac amyloidosis:approaches to diagnosis and management[J]. Cardiol Rev, 2010, 18(1):1-11.
13. KACHOOEI E, MOOSAVI-MOVAHEDI A A, KHODAGHOLI F, et al. Oligomeric forms of insulin amyloid aggregation disrupt outgrowth and complexity of neuron-like PC12 cells[J]. PLoS One, 2012, 7(7):e41344.
14. RAMSHINI H, PARRINI C, RELINI A, et al. Large proteins have a great tendency to aggregate but a low propensity to form amyloid fibrils[J]. PLoS One, 2011,6(1):e16075.
15. PALMIERI L C, MELO-FERREIRA B, BRAGA CA, et al. Stepwise oligomerization of murine amylin and assembly of amyloid fibrils[J]. Biophys Chem, 2013, 180-181:135-144.
16. LEMBRÉ P, VENDRELY C, DI MARTINO P. Amyloid fiber formation by synthetic peptides derived from the sequence of the protein CsgA of Escherichia coli[J]. Protein Pept Lett, 2013, 20(8):942-946.

Journal of Biomedical Engineering

Study on the Formation of Amyloid Fibrils by Self-assembly of an Artificially Designed Peptide GAV-6

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