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Glycine-spacers influence functional motifs exposure and self-assembling propensity of functionalized substrates tailored for neural stem cell cultures.

Taraballi F, Natalello A, Campione M, Villa O, Doglia SM, Paleari A, Gelain F - Front Neuroeng (2010)

Bottom Line: The understanding of phenomena involved in the self-assembling of bio-inspired biomaterials acting as three-dimensional scaffolds for regenerative medicine applications is a necessary step to develop effective therapies in neural tissue engineering.Accordingly, the longer spacer of glycines, the more effective is the functional motif in both eliciting NSCs adhesion, improving their viability and increasing their differentiation.Therefore, optimized designing strategies of functionalized biomaterials may open, in the near future, new therapies in tissue engineering and regenerative medicine.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanomedicine and Tissue Engineering, A.O. Ospedale Niguarda Ca' Granda Milan, Italy.

ABSTRACT
The understanding of phenomena involved in the self-assembling of bio-inspired biomaterials acting as three-dimensional scaffolds for regenerative medicine applications is a necessary step to develop effective therapies in neural tissue engineering. We investigated the self-assembled nanostructures of functionalized peptides featuring four, two or no glycine-spacers between the self-assembly sequence RADA16-I and the functional biological motif PFSSTKT. The effectiveness of their biological functionalization was assessed via in vitro experiments with neural stem cells (NSCs) and their molecular assembly was elucidated via atomic force microscopy, Raman and Fourier Transform Infrared spectroscopy. We demonstrated that glycine-spacers play a crucial role in the scaffold stability and in the exposure of the functional motifs. In particular, a glycine-spacer of four residues leads to a more stable nanostructure and to an improved exposure of the functional motif. Accordingly, the longer spacer of glycines, the more effective is the functional motif in both eliciting NSCs adhesion, improving their viability and increasing their differentiation. Therefore, optimized designing strategies of functionalized biomaterials may open, in the near future, new therapies in tissue engineering and regenerative medicine.

No MeSH data available.


Related in: MedlinePlus

Thermal stability of the self-assembled peptides. Temperature dependence of the intermolecular β-sheet band intensity at 1618 cm−1 of the self-assembly peptides in D2O solution, from 30°C to 100°C. The FPs show a higher stability in comparison with RADA16-I. Noteworthy, 0G-BMHP1 at 100°C reduces its 1618 cm−1 peak intensity at ∼65% similarly to RADA16-I, while 2G-BMHP1 and 4G-BMHP1 at the same temperature decrease to ∼74%. Standard deviation of the data from independent experiments is smaller than the symbol size.
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Figure 5: Thermal stability of the self-assembled peptides. Temperature dependence of the intermolecular β-sheet band intensity at 1618 cm−1 of the self-assembly peptides in D2O solution, from 30°C to 100°C. The FPs show a higher stability in comparison with RADA16-I. Noteworthy, 0G-BMHP1 at 100°C reduces its 1618 cm−1 peak intensity at ∼65% similarly to RADA16-I, while 2G-BMHP1 and 4G-BMHP1 at the same temperature decrease to ∼74%. Standard deviation of the data from independent experiments is smaller than the symbol size.

Mentions: In Figure 5 only 4G-BMHP1 shows a relevant spectral modification related to the buffer conditions. In fact the intensity ratio between peaks at 2940 and 3060 cm−1 is completely interchanged passing from buffer 2 or 3 (i.e. favoring self-assembling) to respectively buffer 1 or 4. The intensity ratio (3061 cm−1/2940 cm−1) in the “not assembling” conditions is ∼1.3 while in the assembling conditions is ∼0.5. The drastic effect on the functional motif in 4G-BMHP1 evinces a larger mobility of the functional motif that makes it more sensitive to the solvent conditions.


Glycine-spacers influence functional motifs exposure and self-assembling propensity of functionalized substrates tailored for neural stem cell cultures.

Taraballi F, Natalello A, Campione M, Villa O, Doglia SM, Paleari A, Gelain F - Front Neuroeng (2010)

Thermal stability of the self-assembled peptides. Temperature dependence of the intermolecular β-sheet band intensity at 1618 cm−1 of the self-assembly peptides in D2O solution, from 30°C to 100°C. The FPs show a higher stability in comparison with RADA16-I. Noteworthy, 0G-BMHP1 at 100°C reduces its 1618 cm−1 peak intensity at ∼65% similarly to RADA16-I, while 2G-BMHP1 and 4G-BMHP1 at the same temperature decrease to ∼74%. Standard deviation of the data from independent experiments is smaller than the symbol size.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2821182&req=5

Figure 5: Thermal stability of the self-assembled peptides. Temperature dependence of the intermolecular β-sheet band intensity at 1618 cm−1 of the self-assembly peptides in D2O solution, from 30°C to 100°C. The FPs show a higher stability in comparison with RADA16-I. Noteworthy, 0G-BMHP1 at 100°C reduces its 1618 cm−1 peak intensity at ∼65% similarly to RADA16-I, while 2G-BMHP1 and 4G-BMHP1 at the same temperature decrease to ∼74%. Standard deviation of the data from independent experiments is smaller than the symbol size.
Mentions: In Figure 5 only 4G-BMHP1 shows a relevant spectral modification related to the buffer conditions. In fact the intensity ratio between peaks at 2940 and 3060 cm−1 is completely interchanged passing from buffer 2 or 3 (i.e. favoring self-assembling) to respectively buffer 1 or 4. The intensity ratio (3061 cm−1/2940 cm−1) in the “not assembling” conditions is ∼1.3 while in the assembling conditions is ∼0.5. The drastic effect on the functional motif in 4G-BMHP1 evinces a larger mobility of the functional motif that makes it more sensitive to the solvent conditions.

Bottom Line: The understanding of phenomena involved in the self-assembling of bio-inspired biomaterials acting as three-dimensional scaffolds for regenerative medicine applications is a necessary step to develop effective therapies in neural tissue engineering.Accordingly, the longer spacer of glycines, the more effective is the functional motif in both eliciting NSCs adhesion, improving their viability and increasing their differentiation.Therefore, optimized designing strategies of functionalized biomaterials may open, in the near future, new therapies in tissue engineering and regenerative medicine.

View Article: PubMed Central - PubMed

Affiliation: Center for Nanomedicine and Tissue Engineering, A.O. Ospedale Niguarda Ca' Granda Milan, Italy.

ABSTRACT
The understanding of phenomena involved in the self-assembling of bio-inspired biomaterials acting as three-dimensional scaffolds for regenerative medicine applications is a necessary step to develop effective therapies in neural tissue engineering. We investigated the self-assembled nanostructures of functionalized peptides featuring four, two or no glycine-spacers between the self-assembly sequence RADA16-I and the functional biological motif PFSSTKT. The effectiveness of their biological functionalization was assessed via in vitro experiments with neural stem cells (NSCs) and their molecular assembly was elucidated via atomic force microscopy, Raman and Fourier Transform Infrared spectroscopy. We demonstrated that glycine-spacers play a crucial role in the scaffold stability and in the exposure of the functional motifs. In particular, a glycine-spacer of four residues leads to a more stable nanostructure and to an improved exposure of the functional motif. Accordingly, the longer spacer of glycines, the more effective is the functional motif in both eliciting NSCs adhesion, improving their viability and increasing their differentiation. Therefore, optimized designing strategies of functionalized biomaterials may open, in the near future, new therapies in tissue engineering and regenerative medicine.

No MeSH data available.


Related in: MedlinePlus