Amyloidogenicity of Small Peptides Although the structure of amyloid fi brils remains

Amyloidogenic Proteins and Peptides

4. Amyloidogenicity of Small Peptides Although the structure of amyloid fi brils remains

limited in atomic detail, there is accumulating evidence from x - ray fi ber diffraction studies that the core of the typical amyloid fi bril is composed of β- sheets whose strands run perpendicular to the fi bril axis (Sunde and Blake 1997 ). It has been shown that specifi c short segments in proteins are responsible for their fi bril - forming behavior. The short peptides of amyloidogneic proteins are able to form a cross - β - structure, which is indistinguish- able from those formed by the usual peptide chains (Lopez De La Paz et al. 2002 ; Jaroniec et al.

2002 ; Petkova et al. 2002 ). Amyloidogenic peptides known to date are summarized in Table 7.2 . Although all mature amyloid fi brils show similar organized structure under x - ray fi ber diffraction, electron microscopy, and specifi c chemical staining analyses, precursor proteins that form amyloid fi brils do not share sequence homology. The tripep- tide VYK is a minimal core segment of fi bril formation among the peptides identifi ed from amyloid proteins (Inouye et al. 2006 ). It is well established that the aromatic residues play an important role in fi brillogenesis (Gazit 2002 ). The interaction between aromatic tyrosine residues is likely initiated to fi bril formation. Besides, phenylalanine pairs occur in the Alzheimer ’ s disease peptide A β because phenylalanine side chains are considered to stabilize the inter- sheet packing. Studies using de novo designed peptides revealed that Ile - Phe dipeptide analog is able to self - assemble as a network of fi brillar struc-

Tau 590 – 595 KVQIIN Pastor et al. 2008

274 – 279 VQIINK Inouye et al. 2006 ; von Bergen et al. 2001

308 – 310 VYK Inouye et al. 2006

307 – 310 IVYK Inouye et al. 2006

305 – 310 VQIVYK Inouye et al. 2006 ; von Bergen et al. 2000

A β 16 – 21 KLVFFA Pastor et al. 2008

16 – 22 KLVFFAE Balbach et al. 2000

37 – 42 GGVVIA Sawaya et al. 2007

35 – 40 MVGGVV Sawaya et al. 2007

Prion human 178 – 183 DCVNIT Pastor et al. 2008

244 – 249 ISFLIF Pastor et al. 2008

245 – 250 SFLIFL Pastor et al. 2008

138 – 144 IIHFGSD Sawaya et al. 2007

170 – 175 SNQNNF Sawaya et al. 2007

Prion mouse 138 – 144 MIHFGND Sawaya et al. 2007

Prion Syrian hamster 138 – 144 MMHFGND Sawaya et al. 2007

Prion elk 170 – 175 NNQNTF Sawaya et al. 2007

Cystatin C human 98 – 103 SFQIYA Pastor et al. 2008

Apolipoprotein A1 13 – 18 LAVLFL Pastor et al. 2008

Calcitonin 15 – 19 DFNKFH Reches et al. 2002

15 – 18 DFNKF Reches et al. 2002

Yeast prion sup35 7 – 13 GNNQQNY Gsponer et al. 2003 ; Balbirnie et al. 2001

8 – 13 NNQQNY Nelson et al. 2005

8 – 11 NNQQ Sawaya et al. 2007

Yeast prion sup35 & huntingtin — QQQQQ Sawaya et al. 2007

β 2 - microglobulin 83 – 88 NHVTLS Ivanova et al. 2004

83 – 89 NHVTLSQ Ivanova et al. 2004

62 – 67 FYLLYY Ivanova et al. 2004 ; Jones et al. 2003

64 – 69 LLYYTE Ivanova et al. 2004 ; Jones et al. 2003

Insulin A chain 13 – 18 LYQLE Sawaya et al. 2007

Insulin B chain 12 – 16 VEALY Sawaya et al. 2007

Lysozyme human 56 – 61 IFQINS Krebs et al. 2000

Lysozyme hen 55 – 60 ILQINS Krebs et al. 2000

IAPP (Amylin) 22 – 27 NFGAIL Tenidis et al. 2000

28 – 33 SSTNVG Tenidis et al. 2000

14 – 20 NFLVHSS Tenidis et al. 2000

RNase 15 – 20 SSTSAA Sawaya et al. 2007

Myoglobin 108 – 113 SQAIIH Fandrich et al. 2003

α - synuclein 51 – 56 GVATVA Sawaya et al. 2007

66 – 74 VGGAVVTGV Sawaya et al. 2007

86 – 92 GSIAAT Sawaya et al. 2007

Designed peptide — KTVIIE Lopez De La Paz et al. 2002

— STVIIE Pastor et al. 2008 ; Lopez De La Paz et al. 2002

— KTVIIT Lopez De La Paz et al. 2002

— STVIIT Lopez De La Paz et al. 2002

— KTVLIE Lopez De La Paz et al. 2002

— KTVIVE Lopez De La Paz et al. 2002

— KTVIYE Lopez De La Paz et al. 2002

— STVIYE Lopez De La Paz et al. 2002

— IIIII Sambasivam et al. 2008

— FF Reches and Gazit 2003

— IF de Groot et al. 2007

The open - interface is also presumed to be stable because of the interaction between the positions 102Y and 106W. The open - interface is thought of as playing an important role to make bigger oligomer or elongate their fi brils. Destabilization of closed - interface open - interface may be effective for preventing nucleation and for preventing elongata- tion of fi brils, respectively. It can be proposed that inhibitors having more compact structure, such as phenol carboxylic acid or phenol amine, may be more effective against nucleation formation but not so for amyloid fi bril elongation. Bindings could be induced by hydrophobic interactions between polyphenol rings and the hydrophobic region of closed - interface, α - β interface in L68Q cystatin C, thus blocking three - dimensional domain swapping and stabilizing the amyloidogenic protein conformation.

The inhibitory mechanism of dopamine is illustrated in Figure 7.2 . Compared with compact molecules, large compounds with double rings such as fl avo- nids or curcumin exerted an inhibitory effect on the amyloid fi bril elongation phase. In this phase, oligomers stack with each other and elongate fi brils by β - interaction with long β - sheets termed open - interface. The cohesive new structural feature could be observed in the dimmer. Large molecules are hypothesized to be involved in inhibiting β -

Figure 7.2. Schematic model for the inhibitory mechanism of amyloid fi bril formation by polyphenol compounds. Left fi gure shows a dimeric domain - swapped L68Q human cystatin C ( http://www.rcsb.org/pdb , PDB ID = 1TIJ).

interactions of open - interface with each oligomer.

These interactions could be reinforced by H - bond between the hydroxyl group of phenolic rings and the donor/acceptor group of open - interface (Figure 7.2 ). These observations may be useful for treatment of amyloidosis.

5.2. Peptidic Compounds

Highly amyloidogenic core sequences in amyloid proteins may play critical roles in the initiation and progression of amyloid fi bril formation (Sawaya et al. 2007 ). Thus, it is postulated that fi brillogenesis of A β can be inhibited by short peptides ’ partially homologous sequence acting as β - sheet breakers (Soto et al. 1996 ). A small peptide, LPFFD, which was designed from A β 17 - 20 (LVFF), behaves as a β - sheet breaker and completely blocks the formation of amyloid fi brils in a rat brain model of amyloidosis (Soto et al. 1998 ). Findeis et al. successfully developed peptidic inhibitors with potent antipolymeriza- tion activity (1999) . On the basis of optimization of the A β - derived peptides portion and size - reduction trials, they found that Cholyl - Leu - Val - Phe - Phe - Ala - OH showed a potent inhibitory activity against amyloid formation. Murphy et al. (2008) proposed synthetic peptidic derivatives for inhibition of

great impact on the development of antiamyloid agents. Indeed, peptidic modulators were developed based on the partially homologous sequence with the core sequences. Several observations demonstrated that polyphenols are capable of inhibiting amyloid fi bril formation in vitro, where it is assumed that some of them act directly with the amyloidogenic core region. These fi ndings must open new strategies for the development of amyloid - formation inhibitors.

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5.3. Others

Recently, Tanaka et al. reported that various disac- charides reduced the formation of polyglutamine aggregates through in vitro screening studies.

Further in vivo experiments established that oral administration of treharose, the most effective disac- charide, inhibited the formation of huntingtin aggregates and extended lifespan in a transgenic mouse model of Huntington ’ s disease (Tanaka et al. 2004 ).

The stabilization of aggregation - prone proteins with carbohydrate may provide a new therapeutic strategy for polyglutamine - mediated pathology because it can block the initial stage of the disease cascade.

6. Conclusion

Under certain environments, soluble proteins and protein fragments (peptides) self - assemble into β - sheet - rich structures (cross - β conformation) and form amyloid. Amyloid causes serious disorders known as amyloidosis, such as Alzheimer ’ s disease, hemodialysis - associated disease, and bovine spon- giform encephalopathies, which are characterized by the transformation of soluble proteins/peptides into aggregated fi brils in different organs and tissues.

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Dalam dokumen Peptides in Food and Health (Halaman 96-104)